LiteFold/InterPro · Datasets at Hugging Face

IPR004432

4,432

Polyketide-type polyunsaturated fatty acid synthase, PfaA

Omega_3_polyunsat_FA_synth

Family

572

false

Members of this entry represent PfaA, which is involved in omega-3 polyunsaturated fatty acid biosynthesis, for example PfaA from the eicosapentaenoic acid biosynthesis operon in Photobacterium profundum SS9. PfaA is found together with PfaB, PfaC, and PfaD, and the functions of the individual polypeptides have not yet...

[]

0

[ "NCBIFAM" ]

[ "TIGR02813" ]

[ "omega_3_PfaA" ]

[ 572 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 567, 5 ]

2

[]

0

true

Family

Polyketide-type polyunsaturated fatty acid synthase, PfaA

Omega_3_polyunsat_FA_synth

1

IPR004433

4,433

2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

MenaQ_synth_MenD

Family

11,618

false

MenD was thought to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH. 2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophospha...

[ "GO:0030976", "GO:0070204", "GO:0009234" ]

[ "thiamine pyrophosphate binding", "2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity", "menaquinone biosynthetic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "PIRSF", "NCBIFAM" ]

[ "MF_01659", "PIRSF004983", "TIGR00173" ]

[ "MenD", "MenD", "menD" ]

[ 11082, 10324, 11048 ]

3

[ "EC", "GP", "GP", "METACYC" ]

[ "2.2.1.9", "GenProp0058", "GenProp1560", "PWY-5837" ]

[ "EC:2.2.1.9", "GP:GenProp0058", "GP:GenProp1560", "METACYC:PWY-5837" ]

4

[ "2jla", "2jlc", "2x7j", "3flm", "3hww", "3hwx", "3lq1", "5ej4", "5ej5", "5ej6", "5ej7", "5ej8", "5ej9", "5eja", "5ejm", "5erx", "5ery", "5esd", "5eso", "5ess", "5esu", "5z2p", "5z2r", "5z2u", "6o04", "6o0g", "6o0j", "6o0n", "7tin", "9dqi", "9dsn", "9dtv"...

34

[ "PUB00083317" ]

[ "17760421" ]

[ "Menaquinone biosynthesis in Escherichia coli: identification of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate as a novel intermediate and re-evaluation of MenD activity." ]

[ 2007 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Halobacteriales", "Siphoviridae sp. ctRlz6", "metagenomes" ]

[ 10240, 797, 330, 1, 250 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 6, 1, 2, 6 ]

4

true

Family

2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase

MenaQ_synth_MenD

2

IPR004434

4,434

Isocitrate dehydrogenase NAD-dependent

Isocitrate_DH_NAD

Family

10,981

false

Several NAD- or NADP-dependent dehydrogenases, including 3-isopropylmalate dehydrogenase, tartrate dehydrogenase, and the multimeric forms of isocitrate dehydrogenase, share a nucleotide binding domain unrelated to that of lactate dehydrogenase and its homologues. These enzymes dehydrogenate their substates at a H-C-OH...

[ "GO:0006099" ]

[ "tricarboxylic acid cycle" ]

[ "biological_process" ]

1

[ "NCBIFAM" ]

[ "TIGR00175" ]

[ "mito_nad_idh" ]

[ 10981 ]

1

[ "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "GenProp0033", "GenProp1693", "R-BTA-71403", "R-CEL-71403", "R-CEL-9837999", "R-DDI-71403", "R-DME-71403", "R-DME-9837999", "R-HSA-1268020", "R-HSA-71403", "R-HSA-9837999", "R-MMU-71403", "R-MMU-9837999", "R-RNO-71403", "R-RNO-9837999", "R-SCE-71403", "R-SPO-71403" ]

[ "GP:GenProp0033", "GP:GenProp1693", "REACTOME:R-BTA-71403", "REACTOME:R-CEL-71403", "REACTOME:R-CEL-9837999", "REACTOME:R-DDI-71403", "REACTOME:R-DME-71403", "REACTOME:R-DME-9837999", "REACTOME:R-HSA-1268020", "REACTOME:R-HSA-71403", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-71403", "REACTOM...

17

[ "3blv", "3blw", "3blx", "5gre", "5grf", "5grh", "5gri", "5grl", "5yvt", "6kde", "6kdf", "6kdy", "6ke3", "6l57", "6l59", "7ce3", "8grb", "8grd", "8grg", "8grh", "8gru", "8gs5" ]

22

[]

0

[]

0

null

[ "Bacteria", "Eukaryota", "marine sediment metagenome" ]

[ 117, 10863, 1 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 14, 4, 5, 5, 11, 9, 2, 10, 20, 2, 2, 17 ]

12

true

Family

Isocitrate dehydrogenase NAD-dependent

Isocitrate_DH_NAD

3

IPR004435

4,435

Molybdopterin-guanine dinucleotide biosynthesis protein B (MobB) domain

MobB_dom

Domain

9,274

false

The MobB domain is similar to that of the urease accessory protein UreG and the hydrogenase accessory protein HypB, both GTP hydrolases involved in loading nickel into the metallocentres of their respective target enzymes. It is involved in the final step of molybdenum-cofactor biosynthesis. While its precise function ...

[ "GO:0005525", "GO:0006777" ]

[ "GTP binding", "Mo-molybdopterin cofactor biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "NCBIFAM" ]

[ "PF03205", "TIGR00176" ]

[ "MobB", "mobB" ]

[ 9274, 8814 ]

2

[ "GP" ]

[ "GenProp0466" ]

[ "GP:GenProp0466" ]

1

[ "1np6", "1p9n", "1xjc", "2f1r", "4nkr", "4oyh" ]

6

[ "PUB00015635", "PUB00015687", "PUB00015921", "PUB00016997", "PUB00034757", "PUB00034758", "PUB00034759" ]

[ "12372836", "9219527", "8528286", "14646116", "12114025", "17198377", "16784786" ]

[ "In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli.", "The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein.", "Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a m...

[ 2002, 1997, 1995, 2003, 2002, 2007, 2006 ]

7

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 581, 8519, 14, 160 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Molybdopterin-guanine dinucleotide biosynthesis protein B (MobB) domain

MobB_dom

4

IPR004436

4,436

Isocitrate dehydrogenase NADP-dependent, monomeric

Isocitrate_DH_NADP_mono

Family

10,136

false

This family of enzymes catalyses the NADP(+)-dependent oxidative decarboxylation of isocitrate to form 2-oxoglutarate, CO2, and NADPH within the Krebs cycle ( ). Thus this enzyme supplies the cell with a key intermediate in energy metabolism, and precursors for biosynthetic pathways. The activity of this enzyme, which ...

[ "GO:0004450", "GO:0006099" ]

[ "isocitrate dehydrogenase (NADP+) activity", "tricarboxylic acid cycle" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]

[ "PF03971", "PIRSF009407", "PTHR36999", "TIGR00178" ]

[ "IDH", "IDH_monmr", "", "monomer_idh" ]

[ 9728, 8950, 10109, 9160 ]

4

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "1.1.1.42", "GenProp0033", "PWY-5913", "PWY-6549", "PWY-6728", "PWY-6969", "PWY-7124", "PWY-7254", "PWY-7268" ]

[ "EC:1.1.1.42", "GP:GenProp0033", "METACYC:PWY-5913", "METACYC:PWY-6549", "METACYC:PWY-6728", "METACYC:PWY-6969", "METACYC:PWY-7124", "METACYC:PWY-7254", "METACYC:PWY-7268" ]

9

[ "1itw", "1j1w", "2b0t", "3mbc", "4zda", "5kvu", "5z16", "6g3u", "7y1u" ]

9

[ "PUB00017001", "PUB00017002" ]

[ "7836312", "12467571" ]

[ "Cloning, sequence analysis, expression, and inactivation of the Corynebacterium glutamicum icd gene encoding isocitrate dehydrogenase and biochemical characterization of the enzyme.", "Structure of the monomeric isocitrate dehydrogenase: evidence of a protein monomerization by a domain duplication." ]

[ 1995, 2002 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 16, 9697, 267, 156 ]

4

[]

0

true

Family

Isocitrate dehydrogenase NADP-dependent, monomeric

Isocitrate_DH_NADP_mono

9

IPR004437

4,437

ParB/RepB/Spo0J partition protein

ParB/RepB/Spo0J

Domain

42,860

false

This domain is found in chromosomal and plasmid partition proteins related to ParB, including Spo0J, RepB, and SopB.

[ "GO:0003677" ]

[ "DNA binding" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR00180" ]

[ "parB_part" ]

[ 42860 ]

1

[]

0

[ "1r71", "1vz0", "3mkw", "3mky", "3mkz", "3vwb", "3w2a", "3w3c", "4umk", "6s6h", "6sdk", "6t1f", "6y93", "7bm8", "7bnk", "7bnr", "7nfu", "7ng0", "7o0n", "7ol9", "8qa8", "8qa9" ]

22

[ "PUB00064883" ]

[ "9054507" ]

[ "Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus." ]

[ 1997 ]

1

[ "IPR003115" ]

[ "IPR037972" ]

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "plasmids", "unclassified sequences" ]

[ 93, 41708, 87, 47, 11, 914 ]

6

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Domain

ParB/RepB/Spo0J partition protein

ParB/RepB/Spo0J

6

IPR004438

4,438

Peptidase M3B, oligoendopeptidase F

Peptidase_M3B

Family

8,188

false

This group of metallopeptidases belong to MEROPS peptidase family M3 (clan MA(E)), the type example being oligoendopeptidase F from Lactococcus lactis. The enzyme hydrolyses peptides of 7 and 17 amino acids with fairly broad specificity. Differences in substrate specificity should be expected in other species. The gene...

[ "GO:0004222", "GO:0006508" ]

[ "metalloendopeptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR00181" ]

[ "pepF" ]

[ 8188 ]

1

[ "EC", "METACYC" ]

[ "3.4.24.-", "PWY-8119" ]

[ "EC:3.4.24.-", "METACYC:PWY-8119" ]

2

[ "2qr4", "3ce2" ]

2

[ "PUB00003579" ]

[ "7674922" ]

[ "Evolutionary families of metallopeptidases." ]

[ 1995 ]

1

[ "IPR045090" ]

[ "IPR034009" ]

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 337, 7812, 10, 29 ]

4

[]

0

true

Family

Peptidase M3B, oligoendopeptidase F

Peptidase_M3B

7

IPR004439

4,439

Isocitrate dehydrogenase NADP-dependent, dimeric, prokaryotic

Isocitrate_DH_NADP_dimer_prok

Family

10,677

false

Bacterial isocitrate dehydrogenases (IDHs) ( ) can be classified into two types on the basis of their subunit structure. One is a homodimer, consisting of subunits of about 40-45kDa, which exists in many bacterial species, including Escherichia coli. The other is a monomer with a molecular mass of 80-100kDa, which has ...

[ "GO:0004450", "GO:0006099" ]

[ "isocitrate dehydrogenase (NADP+) activity", "tricarboxylic acid cycle" ]

[ "molecular_function", "biological_process" ]

2

[ "PANTHER", "NCBIFAM" ]

[ "PTHR43504", "TIGR00183" ]

[ "", "prok_nadp_idh" ]

[ 10675, 8337 ]

2

[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "1.1.1.42", "GenProp0033", "GenProp1267", "PWY-5913", "PWY-6549", "PWY-6728", "PWY-6969", "PWY-7124", "PWY-7254", "PWY-7268" ]

[ "EC:1.1.1.42", "GP:GenProp0033", "GP:GenProp1267", "METACYC:PWY-5913", "METACYC:PWY-6549", "METACYC:PWY-6728", "METACYC:PWY-6969", "METACYC:PWY-7124", "METACYC:PWY-7254", "METACYC:PWY-7268" ]

10

[ "1ai2", "1ai3", "1bl5", "1cw1", "1cw4", "1cw7", "1gro", "1grp", "1hj6", "1hqs", "1idc", "1idd", "1ide", "1idf", "1ika", "1iso", "1p8f", "1pb1", "1pb3", "1sjs", "1tyo", "1v94", "1xgv", "1xkd", "2d4v", "2dht", "2e0c", "2e5m", "2iv0", "3dms", "3icd", "3lcb"...

48

[ "PUB00055420" ]

[ "20549192" ]

[ "Isocitrate dehydrogenase isozymes from a psychrotrophic bacterium, Pseudomonas psychrophila." ]

[ 2010 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 504, 9865, 14, 116, 178 ]

5

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Isocitrate dehydrogenase NADP-dependent, dimeric, prokaryotic

Isocitrate_DH_NADP_dimer_prok

3

IPR004441

4,441

RNA methyltransferase TrmH

rRNA_MeTrfase_TrmH

Family

32,510

false

The TrmH family of RNA methyltransferases are involved in rRNA base modification [ ].

[ "GO:0008173", "GO:0006396" ]

[ "RNA methyltransferase activity", "RNA processing" ]

[ "molecular_function", "biological_process" ]

2

[ "PANTHER", "NCBIFAM" ]

[ "PTHR46429", "TIGR00186" ]

[ "", "rRNA_methyl_3" ]

[ 31513, 24000 ]

2

[ "EC", "REACTOME" ]

[ "2.1.1", "R-HSA-6793080" ]

[ "EC:2.1.1", "REACTOME:R-HSA-6793080" ]

2

[ "1gz0" ]

1

[ "PUB00004439" ]

[ "8265370" ]

[ "SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases." ]

[ 1993 ]

1

[]

[ "IPR016479", "IPR024915" ]

0

2

0

[ "Bacteria", "Caudoviricetes", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]

[ 30739, 2, 1068, 28, 673 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Homo sapiens", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 5, 2, 1, 2, 1, 1, 2 ]

7

true

Family

RNA methyltransferase TrmH

rRNA_MeTrfase_TrmH

9

IPR004443

4,443

YjeF N-terminal domain

YjeF_N_dom

Domain

30,442

false

In bacteria or archaea, YjeF N-terminal domains occur either as single domain proteins or fused with other domains and are commonly associated with enzymes. YjeF N-terminal domains (also known as NAD(P)H-hydrate epimerase) are often fused to a YjeF C-terminal domain. It is a bifunctional enzyme that catalyses the epime...

[]

0

[ "HAMAP", "PFAM", "PROFILE", "NCBIFAM" ]

[ "MF_01966", "PF03853", "PS51385", "TIGR00197" ]

[ "NADHX_epimerase", "YjeF_N", "YJEF_N", "yjeF_nterm" ]

[ 23142, 30217, 30374, 23601 ]

4

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "5.1.99.6", "GenProp1736", "PWY-6938", "PWY-8136", "PWY-8137", "R-CEL-196807", "R-DDI-196807", "R-DME-196807", "R-DME-430039", "R-DRE-196807", "R-DRE-430039", "R-HSA-196807", "R-HSA-430039", "R-MMU-196807", "R-MMU-430039", "R-PFA-196807", "R-RNO-196807", "R-SCE-196807", "R-SCE-43...

[ "EC:5.1.99.6", "GP:GenProp1736", "METACYC:PWY-6938", "METACYC:PWY-8136", "METACYC:PWY-8137", "REACTOME:R-CEL-196807", "REACTOME:R-DDI-196807", "REACTOME:R-DME-196807", "REACTOME:R-DME-430039", "REACTOME:R-DRE-196807", "REACTOME:R-DRE-430039", "REACTOME:R-HSA-196807", "REACTOME:R-HSA-430039",...

20

[ "1jzt", "2ax3", "2dg2", "2o8n", "3d3j", "3d3k", "3k5w", "3rno", "3ro7", "3roe", "3rog", "3rox", "3roz", "3rrb", "3rre", "3rrf", "3rrj", "3rs8", "3rs9", "3rsf", "3rsg", "3rsq", "3rss", "3rt7", "3rt9", "3rta", "3rtb", "3rtc", "3rtd", "3rte", "3rtg", "3ru2"...

33

[ "PUB00043768", "PUB00060794" ]

[ "15257761", "21994945" ]

[ "Novel conserved domains in proteins with predicted roles in eukaryotic cell-cycle regulation, decapping and RNA stability.", "Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair." ]

[ 2004, 2011 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 960, 20439, 8536, 507 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 3, 1, 8, 3, 1, 14, 5, 2, 5, 7, 2, 2, 7 ]

13

true

Domain

YjeF N-terminal domain

YjeF_N_dom

9

IPR004446

4,446

D,D-heptose 1,7-bisphosphate phosphatase

Heptose_bisP_phosphatase

Family

12,939

false

In a number of species, including Escherichia coli, the histidine biosynthetic enzymes imidazole glycerol phosphate dehydratase and histidinol phosphatase are found together in the bifunctional protein HisB. This family represents a protein closely related to the histidinol phosphatase domain of HisB. The protein is fo...

[ "GO:0016791", "GO:0005975" ]

[ "phosphatase activity", "carbohydrate metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PIRSF", "PANTHER", "NCBIFAM" ]

[ "PIRSF004682", "PTHR42891", "TIGR00213" ]

[ "GmhB", "", "GmhB_yaeD" ]

[ 9962, 12873, 3506 ]

3

[ "EC", "EC", "GP", "GP" ]

[ "3.1.3", "3.1.3.82", "GenProp0203", "GenProp1239" ]

[ "EC:3.1.3", "EC:3.1.3.82", "GP:GenProp0203", "GP:GenProp1239" ]

4

[ "2fpr", "2fps", "2fpu", "2fpw", "2fpx", "2gmw", "2o2x", "3esq", "3esr", "3l1u", "3l1v", "3l8e", "3l8f", "3l8g", "3l8h", "4pnh" ]

16

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 60, 12514, 64, 3, 298 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

D,D-heptose 1,7-bisphosphate phosphatase

Heptose_bisP_phosphatase

4

IPR004447

4,447

C-terminal-processing peptidase S41A

Peptidase_S41A

Family

34,983

false

This group of serine peptidases belong to MEROPS peptidase family S41 (clan SM), subfamily S41A (C-terminal processing peptidase). It is a family of C-terminal peptidases with different substrates in different species, including processing of D1 protein of the photosystem II reaction centre in higher plants [ ], and cl...

[ "GO:0008236", "GO:0006508" ]

[ "serine-type peptidase activity", "proteolysis" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM", "CDD" ]

[ "TIGR00225", "cd07560" ]

[ "prc", "Peptidase_S41_CPP" ]

[ 32280, 34952 ]

2

[ "EC" ]

[ "3.4.21" ]

[ "EC:3.4.21" ]

1

[ "1fc6", "1fc7", "1fc9", "1fcf", "4c2c", "4c2d", "4c2e", "4c2f", "4c2g", "4c2h", "4ql6", "5wql", "6iqq", "6iqr", "6iqs", "6iqu", "6vbb", "7rpq", "7rqh", "8sxe", "8sxf", "8sxg", "8sxh", "8xud", "9jr1" ]

25

[ "PUB00015389", "PUB00055073", "PUB00057844", "PUB00057845", "PUB00113567", "PUB00121263", "PUB00122149", "PUB00122150", "PUB00122151" ]

[ "10966643", "15678420", "8702985", "1856173", "10715137", "17551844", "11408480", "8576225", "1729701" ]

[ "Crystal structures of the photosystem II D1 C-terminal processing protease.", "Molecular machines for protein degradation.", "Molecular studies of CtpA, the carboxyl-terminal processing protease for the D1 protein of the photosystem II reaction center in higher plants.", "Cloning, mapping, and characterizati...

[ 2000, 2005, 1996, 1991, 2000, 2007, 2001, 1996, 1992 ]

9

[]

[ "IPR023831", "IPR054621", "IPR054625", "IPR054626", "IPR054628" ]

0

5

0

[ "Bacteria", "Eukaryota", "unclassified Caudoviricetes", "unclassified sequences" ]

[ 32081, 2362, 3, 537 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 14, 1, 8, 12 ]

4

true

Family

C-terminal-processing peptidase S41A

Peptidase_S41A

9

IPR004448

4,448

Nitrate reductas, NapE, periplasmic

Nitrate_reductase_NapE

Family

619

false

NapE, homologous to TorE ( ), is a membrane protein of unknown function that is part of the periplasmic nitrate reductase system; it may be part of the enzyme complex. The periplasmic nitrate reductase allows f or nitrate respiration in anaerobic conditions.

[]

0

[ "NCBIFAM" ]

[ "TIGR02973" ]

[ "nitrate_rd_NapE" ]

[ 619 ]

1

[]

0

[]

0

[]

0

[ "IPR010649" ]

[]

1

0

1

[ "Pseudomonadota" ]

[ 619 ]

1

[]

0

true

Family

Nitrate reductas, NapE, periplasmic

Nitrate_reductase_NapE

8

IPR004449

4,449

Phosphohistidine phosphatase SixA

SixA

Family

4,926

false

Phosphohistidine phosphatase SixA ( ) from Escherichia coli exhibits phosphatase activity towards the HPT domain of the ArcB sensor involved in the multistep His-Asp phosphorelay [ ].

[ "GO:0101006", "GO:0036211", "GO:0005737" ]

[ "protein histidine phosphatase activity", "protein modification process", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "NCBIFAM" ]

[ "TIGR00249" ]

[ "sixA" ]

[ 4926 ]

1

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...

[ "3.1.3.-", "PWY-4702", "PWY-5491", "PWY-6148", "PWY-6352", "PWY-6365", "PWY-6366", "PWY-6368", "PWY-6456", "PWY-6575", "PWY-6627", "PWY-6664", "PWY-6686", "PWY-6720", "PWY-6724", "PWY-6955", "PWY-6990", "PWY-6991", "PWY-7018", "PWY-7119", "PWY-7321", "PWY-7531", "PWY-7771...

[ "EC:3.1.3.-", "METACYC:PWY-4702", "METACYC:PWY-5491", "METACYC:PWY-6148", "METACYC:PWY-6352", "METACYC:PWY-6365", "METACYC:PWY-6366", "METACYC:PWY-6368", "METACYC:PWY-6456", "METACYC:PWY-6575", "METACYC:PWY-6627", "METACYC:PWY-6664", "METACYC:PWY-6686", "METACYC:PWY-6720", "METACYC:PWY-6...

36

[ "1ujb", "1ujc", "3f2i" ]

3

[ "PUB00031795" ]

[ "15670209" ]

[ "Crystal structure of the protein histidine phosphatase SixA in the multistep His-Asp phosphorelay." ]

[ 2005 ]

1

[ "IPR013078" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Bracon brevicornis", "metagenomes" ]

[ 81, 4809, 1, 35 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Phosphohistidine phosphatase SixA

SixA

5

IPR004450

4,450

Threonine synthase-like

Thr_synthase-like

Family

33,337

false

Threonine synthase ( ) is involved in threonine biosynthesis. It catalyses the conversion of O-phospho-L-homoserine and water into L-threonine and orthophosphate, using pyridoxal phosphate as a cofactor. The pyridoxal-phosphate binding site is a Lys (K) residue. The enzyme is distantly related to the serine/threonine d...

[]

0

[ "NCBIFAM" ]

[ "TIGR00260" ]

[ "thrC" ]

[ 33337 ]

1

[ "EC", "GP" ]

[ "4.2.3.1", "GenProp0159" ]

[ "EC:4.2.3.1", "GP:GenProp0159" ]

2

[ "1e5x", "1kl7", "1uim", "1uin", "1v7c", "1vb3", "2c2b", "2c2g", "2d1f", "2zsj", "3aex", "3aey", "3v7n", "4f4f", "6cgq", "6nmx", "8g1y" ]

17

[ "PUB00015327", "PUB00064588" ]

[ "3098560", "17034760" ]

[ "Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase.", "A threonine synthase homolog from a mammalian genome." ]

[ 1986, 2006 ]

2

[]

[ "IPR026260" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1109, 26717, 4912, 599 ]

4

[ "Arabidopsis thaliana", "Danio rerio", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)...

[ 6, 3, 1, 3, 3, 1, 5, 7, 1, 1, 6 ]

11

true

Family

Threonine synthase-like

Thr_synthase-like

6

IPR004453

4,453

Epoxyqueuosine reductase QueG

QueG

Family

16,269

false

Proteins in this family are epoxyqueuosine reductases that catalyse the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr) [ ]. These proteins contain the 4Fe-4S ferredoxins iron-sulphur binding domain.

[ "GO:0016491", "GO:0008033", "GO:0008616" ]

[ "oxidoreductase activity", "tRNA processing", "tRNA queuosine(34) biosynthetic process" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_00916", "PTHR30002", "TIGR00276" ]

[ "QueG", "", "" ]

[ 11373, 16265, 15296 ]

3

[ "EC", "GP", "GP", "METACYC", "METACYC" ]

[ "1.17.99.6", "GenProp0677", "GenProp1400", "PWY-6700", "PWY-8106" ]

[ "EC:1.17.99.6", "GP:GenProp0677", "GP:GenProp1400", "METACYC:PWY-6700", "METACYC:PWY-8106" ]

5

[ "5d08", "5d0a", "5d0b", "5d6s", "5t8y" ]

5

[ "PUB00058202" ]

[ "21502530" ]

[ "Discovery of epoxyqueuosine (oQ) reductase reveals parallels between halorespiration and tRNA modification." ]

[ 2011 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 40, 15724, 73, 432 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Epoxyqueuosine reductase QueG

QueG

4

IPR004454

4,454

HD-related protein

HD-related

Family

139

false

The archaeal proteins containing this domain are as yet uncharacterised and of unknown function.

[]

0

[ "NCBIFAM" ]

[ "TIGR00295" ]

[ "" ]

[ 139 ]

1

[]

0

[]

0

[]

0

[]

0

null

[ "Archaea", "Pseudomonadati", "ecological metagenomes" ]

[ 131, 3, 5 ]

3

[]

0

true

Family

HD-related protein

HD-related

6

IPR004456

4,456

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Pglycerate_mutase_ApgM

Family

4,424

false

This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), it is a metalloenzyme found particularly in archaea and some eubacteria. It is responsible for the interconversion of 2-phosphoglycerate and 3-phosphoglycerate [ ]. It is distantly related to the iPGAM ( ) characteristic of plan...

[ "GO:0003824", "GO:0004619" ]

[ "catalytic activity", "phosphoglycerate mutase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]

[ "PF10143", "PIRSF006392", "PTHR31209", "TIGR00306", "cd16011" ]

[ "PhosphMutase", "IPGAM_arch", "", "apgM", "iPGM_like" ]

[ 4201, 3091, 4351, 2918, 3741 ]

5

[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC" ]

[ "5.4.2.12", "GenProp0691", "GenProp1599", "PWY-1042", "PWY-2221", "PWY-5484", "PWY-5723", "PWY-6142", "PWY-6886", "PWY-6901", "PWY-7003", "PWY-7124", "PWY-7218", "PWY-8362", "PWY-8404" ]

[ "EC:5.4.2.12", "GP:GenProp0691", "GP:GenProp1599", "METACYC:PWY-1042", "METACYC:PWY-2221", "METACYC:PWY-5484", "METACYC:PWY-5723", "METACYC:PWY-6142", "METACYC:PWY-6886", "METACYC:PWY-6901", "METACYC:PWY-7003", "METACYC:PWY-7124", "METACYC:PWY-7218", "METACYC:PWY-8362", "METACYC:PWY-8404...

15

[ "2zkt", "3idd", "3kd8" ]

3

[ "PUB00014397", "PUB00014447", "PUB00014464", "PUB00055097" ]

[ "12076796", "12062435", "12644480", "17576516" ]

[ "Molecular characterization of phosphoglycerate mutase in archaea.", "A divergent archaeal member of the alkaline phosphatase binuclear metalloenzyme superfamily has phosphoglycerate mutase activity.", "Phosphoprotein with phosphoglycerate mutase activity from the archaeon Sulfolobus solfataricus.", "Characte...

[ 2002, 2002, 2003, 2007 ]

4

[]

[ "IPR023665" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 751, 2339, 1024, 310 ]

4

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 11, 3, 7 ]

3

true

Family

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Pglycerate_mutase_ApgM

1

IPR004457

4,457

Zinc finger, ZPR1-type

Znf_ZPR1

Domain

5,538

false

This entry represents ZPR1-type zinc finger domains. ZPR1 is an experimentally proven zinc-binding protein that binds the tyrosine kinase domain of the epidermal growth factor receptor (EGFR); binding is inhibited by EGF stimulation and tyrosine phosphorylation, and activation by EGF is followed by some redistribution ...

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "PFAM", "SMART", "NCBIFAM" ]

[ "PF03367", "SM00709", "TIGR00310" ]

[ "Zn_ribbon_ZPR1", "Zpr1", "ZPR1_znf" ]

[ 5131, 5497, 5107 ]

3

[]

0

[ "2qkd" ]

1

[ "PUB00014077", "PUB00017397", "PUB00035804", "PUB00035805", "PUB00035806", "PUB00035807", "PUB00035812", "PUB00035838", "PUB00035839", "PUB00090578", "PUB00090579", "PUB00103908" ]

[ "12665246", "8650580", "17210253", "15963892", "15718139", "10529348", "11179890", "16648254", "17068332", "23029159", "27411854", "36630955" ]

[ "Zinc fingers--folds for many occasions.", "Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor.", "Sticky fingers: zinc-fingers as protein-recognition motifs.", "Multiple modes of RNA recognition by zinc finger proteins.", "Zinc finger proteins: getting a grip on RNA.", "Zinc fing...

[ 2002, 1996, 2007, 2005, 2005, 1999, 2001, 2006, 2006, 2012, 2016, 2023 ]

12

[]

0

null

[ "Archaea", "Carnobacterium iners", "Eukaryota", "ecological metagenomes" ]

[ 471, 1, 5044, 22 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 17, 1, 1, 1, 5, 8, 1, 2, 4, 1, 1, 8 ]

12

true

Domain

Zinc finger, ZPR1-type

Znf_ZPR1

4

IPR004458

4,458

Translation initiation factor 2, beta subunit

TIF2_bsu_arc

Family

689

false

The archaeal beta subunit has an unfolded N-terminal domain, a mixed α/β core domain and a C-terminal zinc finger [ ]. The N-terminal region is thought to interact with the gamma subunit, while the central and C-terminal domains are thought to provide RNA-binding sites. Archaeal transcription initiation factor 2 is, li...

[ "GO:0003743", "GO:0006413" ]

[ "translation initiation factor activity", "translational initiation" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_00232", "TIGR00311" ]

[ "eIF_2_beta", "aIF-2beta" ]

[ 669, 365 ]

2

[]

0

[ "1nee", "2d74", "2dcu", "2nxu", "2qmu", "3cw2", "3v11", "5jb3", "5jbh", "6sw9", "6swc" ]

11

[ "PUB00017012", "PUB00017013", "PUB00017014" ]

[ "11980477", "11416183", "14978306" ]

[ "Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2beta/eIF5 family of proteins.", "Molecular mechanisms of translation initiation in eukaryotes.", "Structure of the archaeal translation initiation factor aIF2 beta from Metha...

[ 2002, 2001, 2004 ]

3

[ "IPR045196" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 669, 20 ]

2

[]

0

true

Family

Translation initiation factor 2, beta subunit

TIF2_bsu_arc

3

IPR004460

4,460

Acetyl-CoA decarbonylase/synthase complex subunit alpha

CdhA

Family

254

false

The ACDS complex contains five subunits, among which beta possesses an Ni-Fe-S active-site metal cluster, the A-cluster, at which reaction with acetyl-CoA takes place, generating an acetyl-enzyme species poised for C-C bond cleavage [ ]. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta chains with a...

[ "GO:0006084" ]

[ "acetyl-CoA metabolic process" ]

[ "biological_process" ]

1

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_01137", "TIGR00314", "cd01916" ]

[ "CdhA", "cdhA", "ACS_1" ]

[ 221, 254, 99 ]

3

[ "EC", "METACYC", "METACYC" ]

[ "1.2.7.4", "PWY-5372", "PWY-6780" ]

[ "EC:1.2.7.4", "METACYC:PWY-5372", "METACYC:PWY-6780" ]

3

[ "3cf4", "8riu", "9c0q", "9c0r", "9c0s", "9c0t" ]

6

[ "PUB00043435", "PUB00082744", "PUB00082745" ]

[ "14664578", "12464601", "20202935" ]

[ "The A-cluster in subunit beta of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila: Ni and Fe K-edge XANES and EXAFS analyses.", "Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni...

[ 2003, 2003, 2010 ]

3

[ "IPR004137" ]

[]

1

0

1

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 241, 5, 8 ]

3

[]

0

true

Family

Acetyl-CoA decarbonylase/synthase complex subunit alpha

CdhA

2

IPR004461

4,461

CO dehydrogenase/acetyl-CoA synthase complex beta subunit

CO_DH/Ac-CoA_synth_bsu

Family

1,045

false

The carbon monoxide dehydrogenase alpha subunit ( ) catalyses the interconversion of CO and CO2 and the synthesis of acteyl-coA from the methylated corrinoid/iron sulphur protein, CO and CoA. Nomenclature follows the description for Methanosarcina thermophila. The complex is also found in Archaeoglobus fulgidus, not co...

[ "GO:0043885", "GO:0006084" ]

[ "anaerobic carbon-monoxide dehydrogenase activity", "acetyl-CoA metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "PANTHER", "NCBIFAM" ]

[ "PF03598", "PTHR42281", "TIGR00316" ]

[ "CdhC", "", "cdhC" ]

[ 948, 979, 800 ]

3

[ "EC" ]

[ "2.3.1.169" ]

[ "EC:2.3.1.169" ]

1

[ "1mjg", "1oao", "1ru3", "2z8y", "3git", "3i01", "3i04", "3s2x", "5gol", "5h6w", "6x5k", "6ytt", "6yua", "7nyp", "7nys", "7nz5", "7o0d", "7zkj", "7zkk", "7zkv", "8cja", "8cjb", "8cjc", "8cmw", "9c0s", "9c0t", "9fnc", "9fnj", "9fo4", "9fop", "9fox", "9fr0"...

47

[]

0

[]

[ "IPR023432" ]

0

1

0

[ "Archaea", "Bacteria", "unclassified sequences" ]

[ 277, 629, 139 ]

3

[]

0

true

Family

CO dehydrogenase/acetyl-CoA synthase complex beta subunit

CO_DH/Ac-CoA_synth_bsu

9

IPR004462

4,462

Desulfoferrodoxin, N-terminal domain

Desulfoferrodoxin_N

Domain

1,765

false

The desulforedoxin domain is a small non-haem iron domain present in the desulforedoxin (Dx) and desulfoferrodoxin (Superoxide reductase or Dfx) proteins of some archeael and bacterial methanogens and sulfate/sulfur reducers. It constitutes essentially the full length of desulforedoxin, and the N-terminal domain of Des...

[ "GO:0005506" ]

[ "iron ion binding" ]

[ "molecular_function" ]

1

[ "PFAM", "NCBIFAM", "CDD" ]

[ "PF06397", "TIGR00319", "cd00974" ]

[ "Desulfoferrod_N", "desulf_FeS4", "DSRD" ]

[ 1765, 1291, 1137 ]

3

[ "EC" ]

[ "1.15.1.2" ]

[ "EC:1.15.1.2" ]

1

[ "1cfw", "1dcd", "1dfx", "1dhg", "1dxg", "1vzg", "1vzh", "1vzi", "2ji1", "2ji2", "2ji3", "2lk5", "2lk6" ]

13

[ "PUB00015866", "PUB00016112" ]

[ "11128999", "7666420" ]

[ "Desulfoferrodoxin: a modular protein.", "Crystal structure of desulforedoxin from Desulfovibrio gigas determined at 1.8 A resolution: a novel non-heme iron protein structure." ]

[ 2000, 1995 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Cyprideis torosa", "ecological metagenomes" ]

[ 160, 1498, 1, 106 ]

4

[]

0

true

Domain

Desulfoferrodoxin, N-terminal domain

Desulfoferrodoxin_N

6

IPR004463

4,463

UDP-3-O-acyl N-acetylglucosamine deacetylase

UDP-acyl_GlcNac_deAcase

Family

14,804

false

This entry represents the UDP-3-O-N-acetylglucosamine deacetylase family of proteins. UDP-3-O-N-acetylglucosamine deacetylases are zinc-dependent metalloamidases that catalyse the second and committed step in the biosynthesis of lipid A. Lipid A anchors lipopolysaccharide (the major constituent of the outer membrane) i...

[ "GO:0103117", "GO:0009245" ]

[ "UDP-3-O-acyl-N-acetylglucosamine deacetylase activity", "lipid A biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]

[ "MF_00388", "PF03331", "PTHR33694", "TIGR00325" ]

[ "LpxC", "LpxC", "", "lpxC" ]

[ 13343, 14789, 14413, 13357 ]

4

[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC" ]

[ "3.5.1.108", "GenProp0204", "GenProp1290", "PWY-8073", "PWY-8245", "PWY-8283" ]

[ "EC:3.5.1.108", "GP:GenProp0204", "GP:GenProp1290", "METACYC:PWY-8073", "METACYC:PWY-8245", "METACYC:PWY-8283" ]

6

[ "1p42", "1xxe", "1yh8", "1yhc", "2go3", "2go4", "2ier", "2ies", "2j65", "2jt2", "2o3z", "2ves", "3nzk", "3p3c", "3p3e", "3p3g", "3p76", "3ps1", "3ps2", "3ps3", "3u1y", "3uhm", "4fw3", "4fw4", "4fw5", "4fw6", "4fw7", "4is9", "4isa", "4j3d", "4lcf", "4lcg"...

95

[ "PUB00029703", "PUB00032543", "PUB00035690" ]

[ "12819349", "15667205", "17296300" ]

[ "Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis.", "Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design.", "Amphipathic benzoic acid derivatives: synthesis and binding i...

[ 2003, 2005, 2007 ]

3

[]

0

null

[ "Bacteria", "Candidatus Iainarchaeum sp.", "Eukaryota", "unclassified sequences" ]

[ 13542, 1, 931, 330 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 10, 1, 6, 8 ]

4

true

Family

UDP-3-O-acyl N-acetylglucosamine deacetylase

UDP-acyl_GlcNac_deAcase

1

IPR004464

4,464

Fructose-1,6-bisphosphatase class 2/Sedoheputulose-1,7-bisphosphatase

FBPase_class-2/SBPase

Family

12,927

false

Gluconeogenesis is an important metabolic pathway, which produces glucose from noncarbohydrate precursors such as organic acids, fatty acids, amino acids, or glycerol. Fructose-1,6-bisphosphatase, a key enzyme of gluconeogenesis, is found in all organisms, and five different classes of these enzymes have been identifie...

[ "GO:0042132", "GO:0006071", "GO:0006094" ]

[ "fructose 1,6-bisphosphate 1-phosphatase activity", "glycerol metabolic process", "gluconeogenesis" ]

[ "molecular_function", "biological_process", "biological_process" ]

3

[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]

[ "PF03320", "PIRSF004532", "PTHR30447", "TIGR00330", "cd01516" ]

[ "FBPase_glpX", "GlpX", "", "glpX", "FBPase_glpX" ]

[ 12927, 12362, 12890, 12343, 11982 ]

5

[ "EC", "EC", "GP", "GP", "GP", "GP", "METACYC" ]

[ "3.1.3.11", "3.1.3.37", "GenProp0120", "GenProp1306", "GenProp1344", "GenProp1407", "PWY-5484" ]

[ "EC:3.1.3.11", "EC:3.1.3.37", "GP:GenProp0120", "GP:GenProp1306", "GP:GenProp1344", "GP:GenProp1407", "METACYC:PWY-5484" ]

7

[ "1ni9", "2r8t", "3big", "3bih", "3d1r", "3roj", "3rpl", "5a5l", "6ayu", "6ayv", "6ayy", "7js3", "7txa", "7txb", "7txg", "8g5w", "8g5x" ]

17

[ "PUB00046483" ]

[ "19073594" ]

[ "Structural and biochemical characterization of the type II fructose-1,6-bisphosphatase GlpX from Escherichia coli." ]

[ 2009 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 87, 12523, 77, 240 ]

4

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Fructose-1,6-bisphosphatase class 2/Sedoheputulose-1,7-bisphosphatase

FBPase_class-2/SBPase

4

IPR004465

4,465

Ribonucleotide reductase Class Ib, NrdI

RNR_NrdI

Family

7,358

false

Ribonucleotide reductases (RNRs) are enzymes that catalyse the conversion of ribonucleotides to the corresponding deoxyribonucleotides to provide the precursors of DNA synthesis. There are three classes (I-III) of RNRs and four known subclasses within class I RNRs (Ia-Id) [ ], which differ by their metal cofactor, thei...

[ "GO:0010181", "GO:0036211" ]

[ "FMN binding", "protein modification process" ]

[ "molecular_function", "biological_process" ]

2

[ "PFAM", "PIRSF", "PANTHER", "NCBIFAM" ]

[ "PF07972", "PIRSF005087", "PTHR37297", "TIGR00333" ]

[ "Flavodoxin_NdrI", "NrdI", "", "nrdI" ]

[ 7358, 6604, 7283, 5935 ]

4

[ "GP" ]

[ "GenProp0289" ]

[ "GP:GenProp0289" ]

1

[ "1rlj", "2x2o", "2x2p", "2xod", "2xoe", "3n39", "3n3a", "3n3b", "4bmo", "4bmp", "4n82", "6ebq", "7mmp", "7mmq", "7mmr", "7mms", "7z3d", "7z3e", "8j4v", "8j4w", "8j4x", "8j4y" ]

22

[ "PUB00017193", "PUB00100955", "PUB00100956" ]

[ "12686643", "24295378", "30224458" ]

[ "Corynebacterium ammoniagenes class Ib ribonucleotide reductase: transcriptional regulation of an atypical genomic organization in the nrd cluster.", "Crystal structure of Bacillus cereus class Ib ribonucleotide reductase di-iron NrdF in complex with NrdI.", "Metal-free class Ie ribonucleotide reductase from pa...

[ 2003, 2014, 2018 ]

3

[]

[ "IPR020852" ]

0

1

0

[ "Bacteria", "Caudoviricetes", "Eukaryota", "metagenomes" ]

[ 7219, 117, 4, 18 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribonucleotide reductase Class Ib, NrdI

RNR_NrdI

3

IPR004466

4,466

Ribonuclease M5

RNase_M5

Family

4,173

false

Ribonuclease M5 is required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. It cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step [ , ].

[ "GO:0043822" ]

[ "ribonuclease M5 activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01469", "TIGR00334" ]

[ "RNase_M5", "5S_RNA_mat_M5" ]

[ 4133, 4156 ]

2

[ "EC" ]

[ "3.1.26.8" ]

[ "EC:3.1.26.8" ]

1

[ "6tg6", "6tpq", "6z2b" ]

3

[ "PUB00060781", "PUB00060782" ]

[ "4215038", "402365" ]

[ "In vitro maturation of precursors of 5S ribosomal RNA from Bacillus subtilis.", "Partial purification and properties of a ribosomal RNA maturation endonuclease from Bacillus subtilis." ]

[ 1974, 1977 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 4158, 2, 13 ]

3

[]

0

true

Family

Ribonuclease M5

RNase_M5

4

IPR004467

4,467

Orotate phosphoribosyl transferase domain

Or_phspho_trans_dom

Domain

25,662

false

Orotate phosphoribosyltransferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. This entry represents the orotate phosphoribosyl transferase domain.

[ "GO:0004588" ]

[ "orotate phosphoribosyltransferase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR00336" ]

[ "pyrE" ]

[ 25662 ]

1

[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.4.2.10", "GenProp0187", "GenProp1418", "GenProp1614", "PWY-5686", "PWY-7790", "PWY-7791", "R-CEL-500753", "R-DDI-500753", "R-DME-500753", "R-HSA-500753", "R-MMU-500753" ]

[ "EC:2.4.2.10", "GP:GenProp0187", "GP:GenProp1418", "GP:GenProp1614", "METACYC:PWY-5686", "METACYC:PWY-7790", "METACYC:PWY-7791", "REACTOME:R-CEL-500753", "REACTOME:R-DDI-500753", "REACTOME:R-DME-500753", "REACTOME:R-HSA-500753", "REACTOME:R-MMU-500753" ]

12

[ "1lh0", "1opr", "1oro", "1sto", "2aee", "2p1z", "2pry", "2prz", "2ps1", "2wns", "2yzk", "3dez", "3m3h", "3mjd", "3n2l", "3qw4", "4ohc", "4rv4", "4wml", "4wn3", "5hkf", "5hki", "5hkl", "6tai", "6taj", "6tak", "9e5g" ]

27

[]

0

[ "IPR000836" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 887, 19900, 4485, 6, 384 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 4, 2, 1, 1, 1, 6, 3, 1, 1, 4, 2, 1, 8 ]

13

true

Domain

Orotate phosphoribosyl transferase domain

Or_phspho_trans_dom

1

IPR004468

4,468

CTP synthase

CTP_synthase

Family

38,921

false

CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism, catalysing the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position [ ]. The enzyme exists as a dimer which consists of an N-terminal synthetase domain and C-terminal glutaminase domain that aggregates as a tetra...

[ "GO:0003883", "GO:0006221" ]

[ "CTP synthase activity", "pyrimidine nucleotide biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_01227", "PTHR11550", "TIGR00337" ]

[ "PyrG", "", "PyrG" ]

[ 27216, 38911, 33141 ]

3

[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.3.4.2", "GenProp1262", "GenProp1396", "GenProp1635", "PWY-7176", "PWY-7177", "PWY-7185", "R-BTA-499943", "R-DDI-499943", "R-DME-499943", "R-DRE-499943", "R-GGA-499943", "R-HSA-499943", "R-MMU-499943", "R-RNO-499943", "R-SCE-499943", "R-SPO-499943" ]

[ "EC:6.3.4.2", "GP:GenProp1262", "GP:GenProp1396", "GP:GenProp1635", "METACYC:PWY-7176", "METACYC:PWY-7177", "METACYC:PWY-7185", "REACTOME:R-BTA-499943", "REACTOME:R-DDI-499943", "REACTOME:R-DME-499943", "REACTOME:R-DRE-499943", "REACTOME:R-GGA-499943", "REACTOME:R-HSA-499943", "REACTOME:R-...

17

[ "1s1m", "1vcm", "1vcn", "1vco", "2ad5", "2v4u", "2vkt", "2vo1", "2w7t", "3ihl", "3nva", "4zdi", "4zdj", "4zdk", "5n29", "5tkv", "5u03", "5u05", "5u3c", "5u6r", "6l6z", "6lfg", "6pk4", "6pk7", "7dpt", "7dpw", "7mgz", "7mh0", "7mh1", "7mif", "7mig", "7mih"...

66

[ "PUB00007677", "PUB00012378" ]

[ "9711852", "12522217" ]

[ "Linkage of genes encoding enolase (eno) and CTP synthase (pyrG) in the beta-subdivision proteobacterium Nitrosomonas europaea.", "Thr-431 and Arg-433 are part of a conserved sequence motif of the glutamine amidotransferase domain of CTP synthases and are involved in GTP activation of the Lactococcus lactis enzym...

[ 1998, 2003 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 953, 27555, 9558, 9, 846 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 30, 2, 5, 2, 1, 17, 4, 1, 23, 9, 2, 1, 75 ]

13

true

Family

CTP synthase

CTP_synthase

1

IPR004469

4,469

Phosphoserine phosphatase

PSP

Family

19,674

false

Phosphoserine phosphatase ( ), also known as O-phosphoserine phosphohydrolase, is involved in both serine and glycine biosynthesis. It catalyzes the reaction 3-phospho-serine + H2O = L-serine + phosphate, which is the last step in the biosynthesis of serine from carbohydrates. The reaction proceeds via the formation of...

[ "GO:0036424", "GO:0006564" ]

[ "L-phosphoserine phosphatase activity", "L-serine biosynthetic process" ]

[ "molecular_function", "biological_process" ]

2

[ "SFLD", "NCBIFAM" ]

[ "SFLDF00029", "TIGR00338" ]

[ "phosphoserine_phosphatase", "serB" ]

[ 16856, 19670 ]

2

[ "EC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.1.3.3", "R-BTA-977347", "R-DME-977347", "R-HSA-977347", "R-MMU-977347", "R-RNO-977347", "R-SCE-977347", "R-SPO-977347" ]

[ "EC:3.1.3.3", "REACTOME:R-BTA-977347", "REACTOME:R-DME-977347", "REACTOME:R-HSA-977347", "REACTOME:R-MMU-977347", "REACTOME:R-RNO-977347", "REACTOME:R-SCE-977347", "REACTOME:R-SPO-977347" ]

8

[ "1f5s", "1j97", "1l7m", "1l7n", "1l7o", "1l7p", "1l8l", "1l8o", "1nnl", "3m1y", "3n28", "3p96", "4eze", "5is2", "5it0", "5it4", "5jjb", "5jlp", "5jlr", "5jma", "5t41", "6hyj", "6hyy", "6q6j", "7qpl", "8a1z", "8a21", "8q4s", "8qob", "9fq5", "9fqc", "9fqn"...

32

[ "PUB00029151" ]

[ "12777757" ]

[ "High-resolution structure of human phosphoserine phosphatase in open conformation." ]

[ 2003 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctCCX1", "unclassified sequences" ]

[ 579, 15194, 3607, 2, 292 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 3, 7, 1, 1, 1, 3, 1, 1, 5, 2, 1, 1, 4 ]

13

true

Family

Phosphoserine phosphatase

PSP

4

IPR004470

4,470

ZPR1-like, archaea

ZPR1-like_arc

Family

419

false

This entry represents a group of ZPR1-like proteins predominantly found in archaea, including the poorly characterised ZPR1-like proteins PH1223 and MJ0530. ZPR1 was shown experimentally to bind zinc. ZPR1 binds the tyrosine kinase domain of epidermal growth factor receptor [ ] but is displaced by receptor activation a...

[ "GO:0008270" ]

[ "zinc ion binding" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR00340" ]

[ "zpr1_rel" ]

[ 419 ]

1

[]

0

[]

0

[ "PUB00017397", "PUB00103908" ]

[ "8650580", "36630955" ]

[ "Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor.", "Zinc-finger protein Zpr1 is a bespoke chaperone essential for eEF1A biogenesis." ]

[ 1996, 2023 ]

2

[ "IPR040141" ]

[]

1

0

1

[ "Archaea", "ecological metagenomes" ]

[ 406, 13 ]

2

[]

0

true

Family

ZPR1-like, archaea

ZPR1-like_arc

2

IPR004471

4,471

Branched-chain amino acid transport, AzlC

Brnchd-chn_aa_trnsp_AzlC

Family

301

false

The gene encoding the AzlC protein is a part of the azl operon which is involved in branched-chain amino acid transport [ ]. AzlCD is a bipartite histidine exporter consisting of AzlC and AzlD subunits [ ]. Overexpression of this gene results in resistance to a leucine analog, 4-azaleucine.

[ "GO:0016020" ]

[ "membrane" ]

[ "cellular_component" ]

1

[ "NCBIFAM" ]

[ "TIGR00346" ]

[ "azlC" ]

[ 301 ]

1

[]

0

[]

0

[ "PUB00011254", "PUB00152867" ]

[ "9287000", "36377869" ]

[ "An lrp-like gene of Bacillus subtilis involved in branched-chain amino acid transport.", "How To Deal with Toxic Amino Acids: the Bipartite AzlCD Complex Exports Histidine in <i>Bacillus subtilis</i>." ]

[ 1997, 2022 ]

2

[ "IPR011606" ]

[]

1

0

1

[ "Bacteria" ]

[ 301 ]

1

[]

0

true

Family

Branched-chain amino acid transport, AzlC

Brnchd-chn_aa_trnsp_AzlC

8

IPR004472

4,472

Dethiobiotin synthase BioD

DTB_synth_BioD

Family

18,716

false

BioD is involved in biotin biosynthesis and catalyses the reaction (CO2 + 7,8-diaminononanoate + ATP = dethiobiotin + phosphate + ADP) [ ]. It binds ATP and requires magnesium as a co-factor. Proteins in this entry also include bifunctional proteins, such as BioCD from Bordetella avium, BioDA from Aspergillus nidulans ...

[ "GO:0000287", "GO:0004141", "GO:0005524", "GO:0009102" ]

[ "magnesium ion binding", "dethiobiotin synthase activity", "ATP binding", "biotin biosynthetic process" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "PIRSF", "PANTHER", "NCBIFAM" ]

[ "MF_00336", "PIRSF006755", "PTHR43210", "TIGR00347" ]

[ "BioD", "DTB_synth", "", "bioD" ]

[ 18107, 15872, 17579, 17073 ]

4

[ "EC", "GP", "GP", "METACYC" ]

[ "6.3.3.3", "GenProp0036", "GenProp1377", "PWY-7380" ]

[ "EC:6.3.3.3", "GP:GenProp0036", "GP:GenProp1377", "METACYC:PWY-7380" ]

4

[ "1a82", "1bs1", "1byi", "1dad", "1dae", "1daf", "1dag", "1dah", "1dai", "1dak", "1dam", "1dbs", "1dts", "2qmo", "3fgn", "3fmf", "3fmi", "3fpa", "3mle", "3of5", "3qxc", "3qxh", "3qxj", "3qxs", "3qxx", "3qy0", "4a0f", "4a0g", "4a0h", "4a0r", "4wop", "6cve"...

59

[ "PUB00056787", "PUB00085095", "PUB00093987" ]

[ "4921568", "17993549", "20713166" ]

[ "The purification and properties of dethiobiotin synthetase.", "A bifunctional locus (BIO3-BIO1) required for biotin biosynthesis in Arabidopsis.", "Characterization of the Aspergillus nidulans biotin biosynthetic gene cluster and use of the bioDA gene as a new transformation marker." ]

[ 1970, 2008, 2011 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 247, 17005, 1275, 189 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Zea mays" ]

[ 4, 2, 1, 1, 5 ]

5

true

Family

Dethiobiotin synthase BioD

DTB_synth_BioD

3

IPR004473

4,473

Restriction endonuclease, type I, HsdR

Restrct_endonuc_typeI_HsdR

Family

13,367

false

This entry represents the R subunit (HsdR) of type I restriction endonucleases. The restriction subunit (R) is required for both nuclease and ATPase activity, but not for modification. After locating a non-methylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-depend...

[ "GO:0003677", "GO:0005524", "GO:0009035", "GO:0009307" ]

[ "DNA binding", "ATP binding", "type I site-specific deoxyribonuclease activity", "DNA restriction-modification system" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM" ]

[ "TIGR00348" ]

[ "hsdR" ]

[ 13367 ]

1

[ "EC" ]

[ "3.1.21.3" ]

[ "EC:3.1.21.3" ]

1

[ "2w00", "4be7", "4beb", "4bec", "4xjx", "6h2j", "7bst", "7bto", "7btp", "7btq", "7btr" ]

11

[ "PUB00019721", "PUB00019722", "PUB00020851", "PUB00096663", "PUB00099965" ]

[ "11555298", "10449767", "8412658", "32483229", "12654995" ]

[ "Analysis of type I restriction modification systems in the Neisseriaceae: genetic organization and properties of the gene products.", "Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes.", "Conservation of motifs within the unu...

[ 2001, 1999, 1993, 2020, 2003 ]

5

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 395, 12849, 2, 11, 110 ]

5

[]

0

true

Family

Restriction endonuclease, type I, HsdR

Restrct_endonuc_typeI_HsdR

3

IPR004474

4,474

Cell envelope-related transcriptional attenuator domain

LytR_CpsA_psr

Domain

44,940

false

This entry describes a domain (known as LCP domain) that is found in the predicted extracellular domain of a number of proteins involved in cell wall biosynthesis [ ]. One of these is protein Psr, described as a penicillin binding protein 5 (PDP-5) synthesis repressor. Another is Bacillus subtilis LytR, described as a ...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF03816", "TIGR00350" ]

[ "LytR_cpsA_psr", "lytR_cpsA_psr" ]

[ 44939, 41835 ]

2

[ "GP", "GP" ]

[ "GenProp1398", "GenProp1756" ]

[ "GP:GenProp1398", "GP:GenProp1756" ]

2

[ "2xxp", "2xxq", "3mej", "3nro", "3nxh", "3okz", "3owq", "3pe5", "3qfi", "3tel", "3tep", "3tfl", "4de8", "4de9", "4obm", "5v8c", "6mps", "6mpt", "6uex", "6uf3", "6uf5", "6uf6", "8qty", "9cy9", "9gn3" ]

25

[ "PUB00093455" ]

[ "27551018" ]

[ "Impact of LytR-CpsA-Psr Proteins on Cell Wall Biosynthesis in Corynebacterium glutamicum." ]

[ 2016 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Methanobacterium", "Siphoviridae sp. ctHip2", "unclassified sequences" ]

[ 44430, 20, 8, 1, 481 ]

5

[ "Arabidopsis thaliana" ]

[ 1 ]

1

true

Domain

Cell envelope-related transcriptional attenuator domain

LytR_CpsA_psr

4

IPR004475

4,475

DNA polymerase II large subunit DP2

PolC_DP2

Family

1,048

false

This family represents the large subunit, DP2, of a two subunit novel archaebacterial replicative DNA polymerase first characterised for Pyrococcus furiosus [ ]. The orthologue from Methanococcus jannaschii has also been characterised [ ].

[ "GO:0003677", "GO:0003887", "GO:0006260" ]

[ "DNA binding", "DNA-directed DNA polymerase activity", "DNA replication" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "PIRSF", "PANTHER", "NCBIFAM" ]

[ "MF_00324", "PIRSF016275", "PTHR42210", "TIGR00354" ]

[ "DNApol_II_L_arch", "PolC_DP2", "", "polC" ]

[ 780, 570, 1048, 779 ]

4

[ "EC", "EC" ]

[ "2.7.7.7", "3.1.11.1" ]

[ "EC:2.7.7.7", "EC:3.1.11.1" ]

2

[ "3o59", "5ijl", "6hms", "6knb", "6knc", "6t8h", "8ppt", "8ppu", "8ppv", "9f29", "9f2a" ]

11

[ "PUB00085195", "PUB00085196" ]

[ "8787781", "9555910" ]

[ "A non-alpha-like DNA polymerase from the hyperthermophilic archaeon Pyrococcus furiosus.", "A novel DNA polymerase family found in Archaea." ]

[ 1995, 1998 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Geodia barretti", "ecological metagenomes" ]

[ 941, 3, 1, 103 ]

4

[]

0

true

Family

DNA polymerase II large subunit DP2

PolC_DP2

4

IPR004476

4,476

Ribonuclease II/ribonuclease R

RNase_II/RNase_R

Family

21,969

false

This family is defined to identify a pair of paralogous 3'->5' exoribonucleases in Escherichia coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterised originally as required for the expression of virulence genes, but is now recognised as the exoribonuclease ...

[ "GO:0003723", "GO:0004540", "GO:0016070" ]

[ "RNA binding", "RNA nuclease activity", "RNA metabolic process" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR00358" ]

[ "3_prime_RNase" ]

[ 21969 ]

1

[ "EC", "GP" ]

[ "3.1.13.1", "GenProp1360" ]

[ "EC:3.1.13.1", "GP:GenProp1360" ]

2

[ "2id0", "2ix0", "2ix1", "5xgu", "7dcy", "7dic", "7did", "7dol", "8cdu", "8cdv", "8cec", "8ced", "8cee" ]

13

[ "PUB00015537" ]

[ "11948193" ]

[ "Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II." ]

[ 2002 ]

1

[]

[ "IPR011804", "IPR011805" ]

0

2

0

[ "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 21766, 17, 2, 184 ]

4

[ "Escherichia coli (strain K12)" ]

[ 2 ]

1

true

Family

Ribonuclease II/ribonuclease R

RNase_II/RNase_R

6

IPR004477

4,477

ComEC/Rec2-related protein

ComEC_N

Domain

27,085

false

This family is defined to identify a pair of paralogous 3' exoribonucleases in Escherichia coli, plus the set of proteins apparently orthologous to one or the other in other eubacteria. VacB was characterised originally as required for the expression of virulence genes, but is now recognised as the exoribonuclease RNas...

[]

0

[ "PFAM", "NCBIFAM" ]

[ "PF03772", "TIGR00360" ]

[ "Competence", "ComEC_N-term" ]

[ 27085, 26075 ]

2

[]

0

[]

0

[ "PUB00052316" ]

[ "8901420" ]

[ "Who's competent and when: regulation of natural genetic competence in bacteria." ]

[ 1996 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]

[ 26548, 18, 1, 518 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

ComEC/Rec2-related protein

ComEC_N

8

IPR004480

4,480

Monothiol glutaredoxin-related

Monothiol_GRX-rel

Family

21,109

false

Glutaredoxins [ , , ], also known as thioltransferases (disulphide reductases), are small proteins of approximately one hundred amino-acid residues which utilise glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [ ]...

[]

0

[ "PANTHER", "NCBIFAM" ]

[ "PTHR10293", "TIGR00365" ]

[ "", "" ]

[ 21029, 17207 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DDI-1362409", "R-HSA-1362409", "R-HSA-917937", "R-MMU-1362409", "R-SCE-1362409", "R-SPO-1362409" ]

[ "REACTOME:R-DDI-1362409", "REACTOME:R-HSA-1362409", "REACTOME:R-HSA-917937", "REACTOME:R-MMU-1362409", "REACTOME:R-SCE-1362409", "REACTOME:R-SPO-1362409" ]

6

[ "1wik", "1yka", "2lku", "2ltk", "2mma", "2mmz", "2mxn", "2wci", "2wul", "2yan", "3gx8", "3ipz", "3zyw", "5y4u" ]

14

[ "PUB00000560", "PUB00001738", "PUB00002504", "PUB00005575", "PUB00014033", "PUB00015562", "PUB00023503", "PUB00030238", "PUB00053832", "PUB00080925", "PUB00080927" ]

[ "3286320", "3152490", "2668278", "1994586", "14713336", "14962389", "9860827", "10493864", "17415523", "15706083", "15814611" ]

[ "Thioredoxin and glutaredoxin: small multi-functional redox proteins with active-site disulphide bonds.", "Thioredoxin and related proteins in procaryotes.", "Thioredoxin and glutaredoxin systems.", "Vaccinia virus encodes a protein with similarity to glutaredoxins.", "Glutaredoxins: glutathione-dependent r...

[ 1988, 1988, 1989, 1991, 2004, 2004, 1998, 1999, 2007, 2005, 2005 ]

11

[]

[ "IPR014434" ]

0

1

0

[ "Bacteria", "Eukaryota", "Methanobacteriati", "unclassified sequences" ]

[ 9925, 10661, 337, 186 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 17, 3, 3, 2, 1, 4, 6, 2, 11, 9, 3, 2, 49 ]

13

true

Family

Monothiol glutaredoxin-related

Monothiol_GRX-rel

3

IPR004481

4,481

Sodium/potassium/calcium exchanger

K/Na/Ca-exchanger

Family

28,319

false

This entry represents the potassium-dependent sodium/calcium exchanger protein family (NCKX), also known as solute carrier family 24 (SLC24) [ ].

[]

0

[ "PANTHER", "NCBIFAM" ]

[ "PTHR10846", "TIGR00367" ]

[ "", "" ]

[ 28304, 20478 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DME-425561", "R-HSA-2485179", "R-HSA-425561", "R-HSA-5619036", "R-HSA-5619055", "R-HSA-5619077", "R-MMU-425561", "R-RNO-425561" ]

[ "REACTOME:R-DME-425561", "REACTOME:R-HSA-2485179", "REACTOME:R-HSA-425561", "REACTOME:R-HSA-5619036", "REACTOME:R-HSA-5619055", "REACTOME:R-HSA-5619077", "REACTOME:R-MMU-425561", "REACTOME:R-RNO-425561" ]

8

[ "3v5s", "3v5u", "5hwx", "5hwy", "5hxc", "5hxe", "5hxh", "5hxr", "5hxs", "5hya", "5jdf", "5jdg", "5jdh", "5jdl", "5jdm", "5jdn", "5jdq" ]

17

[ "PUB00062389", "PUB00062390", "PUB00062391", "PUB00062392", "PUB00062393", "PUB00066789", "PUB00072069" ]

[ "10608890", "16357253", "10662833", "10545508", "18166528", "22287543", "23506883" ]

[ "The retinal rod Na(+)/Ca(2+),K(+) exchanger contains a noncleaved signal sequence required for translocation of the N terminus.", "SLC24A5, a putative cation exchanger, affects pigmentation in zebrafish and humans.", "Molecular cloning and functional expression of the potassium-dependent sodium-calcium exchang...

[ 1999, 2005, 2000, 1999, 2008, 2012, 2013 ]

7

[]

[ "IPR004817" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1406, 14078, 12484, 351 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]

[ 4, 38, 19, 1, 13, 14, 1, 20 ]

8

true

Family

Sodium/potassium/calcium exchanger

K/Na/Ca-exchanger

3

IPR004482

4,482

Mg chelatase-related protein

Mg_chelat-rel

Family

20,855

false

This family of proteins are variously described as 'hypothetical protein yifB', 'competence protein', 'hypothetical protein' or 'Mg chelatase-related protein'. Sequence comparison shows that YifB is closest to the chelatase family [ ]. This family includes ComM, a protein that is induced during competence development [...

[]

0

[ "NCBIFAM" ]

[ "TIGR00368" ]

[ "" ]

[ 20855 ]

1

[]

0

[ "8rxd", "8rxk", "8rxs", "8rxt" ]

4

[ "PUB00014778", "PUB00076551" ]

[ "15037234", "9457884" ]

[ "Evolutionary history and higher order classification of AAA+ ATPases.", "A new transformation-deficient mutant of Haemophilus influenzae Rd with normal DNA uptake." ]

[ 2004, 1998 ]

2

[ "IPR045006" ]

[]

1

0

1

[ "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 20447, 2, 45, 361 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Mg chelatase-related protein

Mg_chelat-rel

2

IPR004484

4,484

Cobyrinate/Hydrogenobyrinate a,c-diamide synthase CbiA/CobB

CbiA/CobB_synth

Family

14,222

false

This family describes cobyrinic acid a,c-diamide synthase CbiA protein of cobalamin biosynthesis. It is responsible for the amidation of cobyrinic acid to cobyrinic acid a,c-diamide via the intermediate formation of cobyrinic acid c-monoamide or hydrogenobrynic acid. NH(2) groups are provided by glutamine and one molec...

[ "GO:0042242" ]

[ "cobyrinic acid a,c-diamide synthase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM", "PANTHER", "NCBIFAM" ]

[ "MF_00027", "NF002204", "PTHR43873", "TIGR00379" ]

[ "CobB_CbiA", "PRK01077.1", "", "cobB" ]

[ 11175, 13488, 14219, 11242 ]

4

[ "EC", "EC", "GP", "METACYC" ]

[ "6.3.5", "6.3.5.11", "GenProp0275", "PWY-7377" ]

[ "EC:6.3.5", "EC:6.3.5.11", "GP:GenProp0275", "METACYC:PWY-7377" ]

4

[]

0

[ "PUB00015238", "PUB00033892", "PUB00153010" ]

[ "10966576", "2172209", "37620358" ]

[ "The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase.", "Purification and characterization of cobyrinic acid a,c-diamide synthase from Pseudomonas denitrificans.", "A synthetic cell-free 36-enzy...

[ 2000, 1990, 2023 ]

3

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "metagenomes" ]

[ 990, 12893, 146, 193 ]

4

[]

0

true

Family

Cobyrinate/Hydrogenobyrinate a,c-diamide synthase CbiA/CobB

CbiA/CobB_synth

3

IPR004485

4,485

Cobalamin biosynthesis CobD/CbiB

Cobalamin_biosynth_CobD/CbiB

Family

16,093

false

This entry represents the CbiB protein, which is involved in cobalamin biosynthesis and porphyrin biosynthesis. It converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. It is part of the cob operon [ ]. Cobalamin (vitamin B12) is a structurally complex cofactor, consisting of a...

[ "GO:0048472", "GO:0009236", "GO:0016020" ]

[ "threonine-phosphate decarboxylase activity", "cobalamin biosynthetic process", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "PFAM", "PANTHER", "NCBIFAM" ]

[ "MF_00024", "PF03186", "PTHR34308", "TIGR00380" ]

[ "CobD_CbiB", "CobD_Cbib", "", "cobal_cbiB" ]

[ 14781, 16084, 15481, 12640 ]

4

[ "GP" ]

[ "GenProp0269" ]

[ "GP:GenProp0269" ]

1

[]

0

[ "PUB00009744", "PUB00014672", "PUB00015657", "PUB00035308", "PUB00035309", "PUB00035310", "PUB00035314", "PUB00070131" ]

[ "11215515", "11153269", "12869542", "17163662", "16042605", "12055304", "14645280", "23922391" ]

[ "Biosynthesis of cobalamin (vitamin B12): a bacterial conundrum.", "Multiple biosynthetic pathways for vitamin B12: variations on a central theme.", "Comparative genomics of the vitamin B12 metabolism and regulation in prokaryotes.", "B12 trafficking in mammals: A for coenzyme escort service.", "Aerobic syn...

[ 2000, 2001, 2003, 2006, 2005, 2002, 2003, 2013 ]

8

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 781, 15084, 38, 190 ]

4

[]

0

true

Family

Cobalamin biosynthesis CobD/CbiB

Cobalamin_biosynth_CobD/CbiB

5

IPR004486

4,486

CO dehydrogenase/acetyl-CoA synthase delta subunit

CO_DH/Ac-CoA_synth_dsu

Family

261

false

This is the small subunit of the ACDS complex that catalyses the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. ACDS complex is a heterodimer which catalyses the reaction CO + H2O + Acceptor = CO2 + Reduced acceptor and is involved in the synthesis of acetyl-CoA from ...

[ "GO:0006730" ]

[ "one-carbon metabolic process" ]

[ "biological_process" ]

1

[ "HAMAP", "NCBIFAM" ]

[ "MF_01135", "TIGR00381" ]

[ "CdhD", "cdhD" ]

[ 188, 261 ]

2

[]

0

[ "4djd", "4dje", "4djf" ]

3

[]

0

[]

0

null

[ "Archaea", "Bacteria", "ecological metagenomes" ]

[ 221, 33, 7 ]

3

[]

0

true

Family

CO dehydrogenase/acetyl-CoA synthase delta subunit

CO_DH/Ac-CoA_synth_dsu

2

IPR004487

4,487

Clp protease, ATP-binding subunit ClpX

Clp_protease_ATP-bd_su_ClpX

Family

27,705

false

ClpX is a member of the HSP (heat-shock protein) 100 family. Gel filtration and electron microscopy showed that ClpX subunits associate to form a six-membered ring that is stabilised by binding of ATP or nonhydrolysable analogs of ATP [ ]. It functions as an ATP-dependent [ ] molecular chaperone and is the regulatory s...

[ "GO:0005524", "GO:0051082", "GO:0140662", "GO:0006457" ]

[ "ATP binding", "unfolded protein binding", "ATP-dependent protein folding chaperone", "protein folding" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM" ]

[ "TIGR00382" ]

[ "clpX" ]

[ 27705 ]

1

[ "GP", "GP", "REACTOME", "REACTOME", "REACTOME" ]

[ "GenProp0251", "GenProp1108", "R-HSA-9837999", "R-MMU-9837999", "R-RNO-9837999" ]

[ "GP:GenProp0251", "GP:GenProp1108", "REACTOME:R-HSA-9837999", "REACTOME:R-MMU-9837999", "REACTOME:R-RNO-9837999" ]

5

[ "1um8", "3hte", "3hws", "4i34", "4i4l", "4i5o", "4i63", "4i81", "4i9k", "6po1", "6po3", "6pod", "6pos", "6pp5", "6pp6", "6pp7", "6pp8", "6ppe", "6sfw", "6vfs", "6vfx", "6wr2", "6wrf", "6wsg", "8e7v", "8e8q", "8e91", "8et3", "8v9r", "8yd0", "9c87", "9c88"...

36

[ "PUB00011891", "PUB00011892", "PUB00011897", "PUB00015582" ]

[ "12925799", "12667450", "12937164", "9575205" ]

[ "Purification, crystallization and preliminary X-ray studies of ClpX from Helicobacter pylori.", "Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals.", "The N-terminal zinc binding domain of ClpX is a dimerization domain that modulates the chaperone...

[ 2003, 2003, 2003, 1998 ]

4

[]

[ "IPR046425" ]

0

1

0

[ "Bacteria", "Caudoviricetes", "Eukaryota", "Methanobrevibacter millerae", "unclassified sequences" ]

[ 24022, 13, 3205, 1, 464 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Zea mays" ]

[ 14, 2, 3, 1, 1, 1, 12, 6, 36 ]

9

true

Family

Clp protease, ATP-binding subunit ClpX

Clp_protease_ATP-bd_su_ClpX

1

IPR004488

4,488

Magnesium/cobalt transport protein CorA

Mg/Co-transport_prot_CorA

Family

13,136

false

The CorA transport system is a primary Mg2+ transporter for Bacteria and Archaea. Some members in this family may have a function other than Mg2+ transport [ ]. Prokaryotic CorA can be classified into two sub-groups: (1) T. maritima type (group A) (2) E. coli and S.typhimurium type (group B) [ ].

[ "GO:0015087", "GO:0015095", "GO:0006824", "GO:0015693", "GO:0016020" ]

[ "cobalt ion transmembrane transporter activity", "magnesium ion transmembrane transporter activity", "cobalt ion transport", "magnesium ion transport", "membrane" ]

[ "molecular_function", "molecular_function", "biological_process", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR00383" ]

[ "corA" ]

[ 13136 ]

1

[]

0

[ "2bbj", "2hn1", "2hn2", "2iub", "3jcf", "3jcg", "3jch", "4cy4", "4eeb", "4eed", "4egw", "4ev6", "4i0u", "5jrw", "5jtg", "5n77", "5n78", "8tmb", "8tmc", "8tmd", "8tme", "8tmf", "8tmg", "8tmh", "8tmi", "8tmj", "8tmk", "8tml", "8tmm", "8tmn", "8tmo", "8tmp"...

33

[ "PUB00003584", "PUB00041779", "PUB00065208", "PUB00072750", "PUB00072751", "PUB00072756", "PUB00072757" ]

[ "9775386", "16857941", "23425532", "15231793", "16835234", "12206392", "17619822" ]

[ "The CorA magnesium transporter gene family.", "Crystal structure of a divalent metal ion transporter CorA at 2.9 angstrom resolution.", "Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport.", "The CorA Mg2+ transporter is...

[ 1998, 2006, 2013, 2004, 2006, 2002, 2007 ]

7

[ "IPR002523" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 406, 12566, 92, 72 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Magnesium/cobalt transport protein CorA

Mg/Co-transport_prot_CorA

3

IPR004489

4,489

Succinate dehydrogenase/fumarate reductase iron-sulphur protein

Succ_DH/fum_Rdtase_Fe-S

Family

29,604

false

Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 ( ). In Escherichia coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydroge...

[ "GO:0016491", "GO:0006099" ]

[ "oxidoreductase activity", "tricarboxylic acid cycle" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR00384" ]

[ "dhsB" ]

[ 29604 ]

1

[ "EC", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "1.3.5.1", "GenProp0033", "GenProp0756", "GenProp1112", "GenProp1143", "GenProp1267", "GenProp1391", "GenProp1493", "GenProp1515", "GenProp1537", "GenProp1672", "GenProp1693", "PWY-3781", "PWY-4302", "PWY-5392", "PWY-561", "PWY-5690", "PWY-5913", "PWY-6728", "PWY-6969", "PWY-...

[ "EC:1.3.5.1", "GP:GenProp0033", "GP:GenProp0756", "GP:GenProp1112", "GP:GenProp1143", "GP:GenProp1267", "GP:GenProp1391", "GP:GenProp1493", "GP:GenProp1515", "GP:GenProp1537", "GP:GenProp1672", "GP:GenProp1693", "METACYC:PWY-3781", "METACYC:PWY-4302", "METACYC:PWY-5392", "METACYC:PWY-5...

39

[ "1e7p", "1kf6", "1kfy", "1l0v", "1nek", "1nen", "1qlb", "1yq3", "1yq4", "1zoy", "1zp0", "2acz", "2b76", "2bs2", "2bs3", "2bs4", "2fbw", "2h88", "2h89", "2wdq", "2wdr", "2wdv", "2wp9", "2wqy", "2ws3", "2wu2", "2wu5", "3abv", "3ae1", "3ae2", "3ae3", "3ae4"...

97

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 775, 22231, 6139, 459 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 12, 2, 1, 3, 2, 10, 4, 2, 6, 8, 1, 1, 20 ]

13

true

Family

Succinate dehydrogenase/fumarate reductase iron-sulphur protein

Succ_DH/fum_Rdtase_Fe-S

5

IPR004490

4,490

Glycolate oxidase subunit GlcD

GlcD

Family

1,916

false

The glc locus of Escherichia coli encodes the subunits of glycolate oxidase and the glc regulator protein. The subunit GlcD is similar to that of several D-lactate dehydrogenases, including that of E. coli. Glycolate oxidase has been found to have some D-lactate dehydrogenase activity.

[ "GO:0003973", "GO:0009339" ]

[ "(S)-2-hydroxy-acid oxidase activity", "glycolate oxidase complex" ]

[ "molecular_function", "cellular_component" ]

2

[ "NCBIFAM" ]

[ "TIGR00387" ]

[ "glcD" ]

[ 1916 ]

1

[ "EC", "GP", "GP", "GP", "METACYC", "METACYC", "METACYC" ]

[ "1.1.99.14", "GenProp1297", "GenProp1374", "GenProp1556", "PWY-6649", "PWY-8362", "PWY-8363" ]

[ "EC:1.1.99.14", "GP:GenProp1297", "GP:GenProp1374", "GP:GenProp1556", "METACYC:PWY-6649", "METACYC:PWY-8362", "METACYC:PWY-8363" ]

7

[]

0

[]

0

[]

0

null

[ "Archaeoglobus fulgidus", "Bacteria", "ecological metagenomes" ]

[ 3, 1911, 2 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Glycolate oxidase subunit GlcD

GlcD

2

IPR004491

4,491

Heat shock protein HslU

HslU

Family

14,130

false

This family of proteins represent HslU, a bacterial clpX homologue, which is an ATPase and chaperone belonging to the AAA Clp/Hsp100 family and a component of the eubacterial proteasome.

[ "GO:0005524", "GO:0008233", "GO:0016887", "GO:0009376" ]

[ "ATP binding", "peptidase activity", "ATP hydrolysis activity", "HslUV protease complex" ]

[ "molecular_function", "molecular_function", "molecular_function", "cellular_component" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_00249", "TIGR00390" ]

[ "HslU", "hslU" ]

[ 11943, 14128 ]

2

[ "GP", "GP" ]

[ "GenProp0835", "GenProp1173" ]

[ "GP:GenProp0835", "GP:GenProp1173" ]

2

[ "1do0", "1do2", "1e94", "1g3i", "1g41", "1g4a", "1g4b", "1hqy", "1ht1", "1ht2", "1im2", "1kyi", "1ofh", "1ofi", "1yyf", "5ji2", "5ji3", "5txv", "6kww", "6pxi", "6pxk", "6pxl", "7mhb" ]

23

[ "PUB00011906" ]

[ "12446803" ]

[ "Eubacterial HslV and HslU subunits homologs in primordial eukaryotes." ]

[ 2002 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 13440, 523, 167 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Heat shock protein HslU

HslU

4

IPR004493

4,493

Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic

Leu-tRNA-synth_Ia_arc/euk

Family

8,402

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000166", "GO:0004823", "GO:0005524", "GO:0006429" ]

[ "nucleotide binding", "leucine-tRNA ligase activity", "ATP binding", "leucyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "PANTHER", "NCBIFAM" ]

[ "PTHR45794", "TIGR00395" ]

[ "", "leuS_arch" ]

[ 8402, 5420 ]

2

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.4", "GenProp0258", "R-DDI-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-9856649", "R-MMU-9856649" ]

[ "EC:6.1.1.4", "GP:GenProp0258", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]

7

[ "1wkb", "1wz2", "2wfd", "2wfe", "2wfg", "3pz6", "5agh", "5agi", "5agj", "5fo4", "5foc", "5fod", "5fof", "5fog", "5fol", "5fom", "5fon", "6kid", "6kie", "6kqy", "6kr7", "6lpf", "6lr6" ]

23

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[]

[ "IPR020791" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "Mimiviridae", "unclassified sequences" ]

[ 800, 4, 7510, 12, 76 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 9, 1, 1, 3, 24, 9, 1, 11, 4, 1, 1, 8 ]

12

true

Family

Leucyl-tRNA synthetase, class Ia, archaeal/eukaryotic cytosolic

Leu-tRNA-synth_Ia_arc/euk

1

IPR004494

4,494

MauM/NapG ferredoxin-type protein

MauM_NapG

Family

1,767

false

MauM ferredoxin-type protein is involved in methylamine utilization [ ]. NapG ferredoxin-type protein is associated with nitrate reductase activity [ ]. The two proteins are highly similar.

[]

0

[ "NCBIFAM" ]

[ "TIGR00397" ]

[ "mauM_napG" ]

[ 1767 ]

1

[ "GP" ]

[ "GenProp1504" ]

[ "GP:GenProp1504" ]

1

[]

0

[ "PUB00007706", "PUB00088159" ]

[ "9202457", "14674886" ]

[ "Organization of methylamine utilization genes (mau) in 'Methylobacillus flagellatum ' KT and analysis of mau mutants.", "NapGH components of the periplasmic nitrate reductase of Escherichia coli K-12: location, topology and physiological roles in quinol oxidation and redox balancing." ]

[ 1997, 2004 ]

2

[]

0

null

[ "Bacteria", "Durusdinium trenchii", "ecological metagenomes" ]

[ 1744, 1, 22 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

MauM/NapG ferredoxin-type protein

MauM_NapG

2

IPR004495

4,495

Methionyl-tRNA synthetase, beta subunit, C-terminal

Met-tRNA-synth_bsu_C

Domain

18,169

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000166", "GO:0004825", "GO:0005524", "GO:0006431" ]

[ "nucleotide binding", "methionine-tRNA ligase activity", "ATP binding", "methionyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "NCBIFAM", "CDD" ]

[ "TIGR00399", "cd02800" ]

[ "metG_C_term", "tRNA_bind_EcMetRS_like" ]

[ 16513, 17867 ]

2

[ "EC", "GP" ]

[ "6.1.1.10", "GenProp0258" ]

[ "EC:6.1.1.10", "GP:GenProp0258" ]

2

[ "1mkh", "1pyb", "1rqg", "2cwp", "6wq6", "6wqi", "7d8r", "7d8s", "7d8t", "8vtz", "8vu0", "9shc" ]

12

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00010727", "PUB00011003", "PUB00030021", "PUB00079872", "PUB00079873", "PUB00080759" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "12390027", "10369686", "11101501", "10704480", "12458790", "12481025" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2002, 1999, 2000, 2000, 2002, 2002 ]

13

[ "IPR002547" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]

[ 888, 17005, 30, 1, 245 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Methionyl-tRNA synthetase, beta subunit, C-terminal

Met-tRNA-synth_bsu_C

3

IPR004496

4,496

Ferredoxin-type protein NapF

NapF

Family

2,438

false

Periplasmic nitrate reductase (NapABC enzyme) is responsible for nitrate dissimilation [ ]. NapF protein is the auxiliary protein of the Nap systems. It interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation [ ].

[ "GO:0051539" ]

[ "4 iron, 4 sulfur cluster binding" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_02201", "TIGR00402", "cd10564" ]

[ "NapF", "napF", "NapF_like" ]

[ 1865, 2114, 2301 ]

3

[]

0

[]

0

[ "PUB00045591", "PUB00088656" ]

[ "17074894", "11450112" ]

[ "The NapF protein of the Escherichia coli periplasmic nitrate reductase system: demonstration of a cytoplasmic location and interaction with the catalytic subunit, NapA.", "Nitrate reduction in the periplasm of gram-negative bacteria." ]

[ 2006, 2001 ]

2

[]

0

null

[ "Bacteria", "ecological metagenomes" ]

[ 2420, 18 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ferredoxin-type protein NapF

NapF

6

IPR004497

4,497

NAD(P)H-quinone oxidoreductase subunit I

NDHI

Family

13,554

false

NAD(P)H-quinone oxidoreductase subunit I ( ) catalyses the conversion of plastoquinone and NADH to plastoquinol and NAD(+). The enzyme binds two 4Fe-4S clusters at iron-sulphur centres which are similar to those of the bacterial-type 4FE-4S ferredoxins.

[ "GO:0008137" ]

[ "NADH dehydrogenase (ubiquinone) activity" ]

[ "molecular_function" ]

1

[ "PANTHER", "NCBIFAM" ]

[ "PTHR47275", "TIGR00403" ]

[ "", "ndhI" ]

[ 13532, 13040 ]

2

[ "EC" ]

[ "7.1.1.-" ]

[ "EC:7.1.1.-" ]

1

[ "6hum", "6khi", "6khj", "6l7o", "6l7p", "6nbq", "6nbx", "6nby", "6tjv", "7eu3", "7f9o", "7wfg", "7wg5", "9grx" ]

14

[]

0

[ "IPR010226" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Viruses", "ecological metagenomes" ]

[ 407, 13141, 3, 3 ]

4

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 3, 2 ]

3

true

Family

NAD(P)H-quinone oxidoreductase subunit I

NDHI

3

IPR004498

4,498

Ribosomal protein L11 methyltransferase

Ribosomal_PrmA_MeTrfase

Family

19,278

false

Ribosomal protein L11 methyltransferase (PrmA) ( ) is required for the methylation of ribosomal protein L11. It forms a bifunctional operon in Escherichia coli with panF (pantothenate transport). In E. coli, it trimethylates the N-terminal alpha-amino group and the ε-amino groups of Lys3 and Lys39 [ ]. In Arabidopsis i...

[ "GO:0008276", "GO:0006479" ]

[ "protein methyltransferase activity", "protein methylation" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "PIRSF", "NCBIFAM" ]

[ "MF_00735", "PIRSF000401", "TIGR00406" ]

[ "Methyltr_PrmA", "RPL11_MTase", "prmA" ]

[ 18887, 15359, 12466 ]

3

[ "EC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC"...

[ "2.1.1.-", "PWY-1061", "PWY-2083", "PWY-3542", "PWY-4021", "PWY-4161", "PWY-4202", "PWY-5059", "PWY-5105", "PWY-5301", "PWY-5305", "PWY-5479", "PWY-5665", "PWY-5729", "PWY-5748", "PWY-5765", "PWY-5773", "PWY-5846", "PWY-5883", "PWY-5975", "PWY-5987", "PWY-601", "PWY-6045"...

[ "EC:2.1.1.-", "METACYC:PWY-1061", "METACYC:PWY-2083", "METACYC:PWY-3542", "METACYC:PWY-4021", "METACYC:PWY-4161", "METACYC:PWY-4202", "METACYC:PWY-5059", "METACYC:PWY-5105", "METACYC:PWY-5301", "METACYC:PWY-5305", "METACYC:PWY-5479", "METACYC:PWY-5665", "METACYC:PWY-5729", "METACYC:PWY-5...

146

[ "1ufk", "2nxc", "2nxe", "2nxj", "2nxn", "2zbp", "2zbq", "2zbr", "3cjq", "3cjr", "3cjt", "3egv" ]

12

[ "PUB00051026", "PUB00095676" ]

[ "18611379", "26116422" ]

[ "Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.", "Dual Targeting of the Protein Methyltransferase PrmA Contributes to Both Chloroplastic and Mitochondrial Ribosomal Protein L11 Methylation in Arabidopsis." ]

[ 2008, 2015 ]

2

[]

0

null

[ "Bacteria", "Eukaryota", "Marine Group I thaumarchaeote", "unclassified sequences" ]

[ 18549, 537, 1, 191 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 5, 1, 4, 2 ]

4

true

Family

Ribosomal protein L11 methyltransferase

Ribosomal_PrmA_MeTrfase

7

IPR004499

4,499

Proline-tRNA ligase, class IIa, archaeal-type

Pro-tRNA-ligase_IIa_arc-type

Family

17,018

false

Proline-tRNA ligase (also known as Prolyl-tRNA synthetase) is a class II tRNA ligase and is recognised by , which recognises tRNA ligases for Gly, His, Ser, and Pro. The proline-tRNA ligases are divided into two widely divergent families. This family includes the archaeal enzyme, the Pro-specific domain of a human mult...

[ "GO:0004827", "GO:0005524", "GO:0006433", "GO:0005737" ]

[ "proline-tRNA ligase activity", "ATP binding", "prolyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_01571", "PTHR43382", "TIGR00408" ]

[ "Pro_tRNA_synth_type3", "", "proS_fam_I" ]

[ 14023, 16985, 13922 ]

3

[ "EC", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.15", "GenProp0258", "R-DME-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-6782315", "R-HSA-9856649", "R-MMU-9856649" ]

[ "EC:6.1.1.15", "GP:GenProp0258", "REACTOME:R-DME-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]

8

[ "1h4q", "1h4s", "1h4t", "1hc7", "1nj1", "1nj2", "1nj5", "1nj6", "1nj8", "3ial", "4hvc", "4k86", "4k87", "4k88", "4ncx", "4olf", "4q15", "4twa", "4wi1", "4ydq", "5f9y", "5f9z", "5ifu", "5v58", "5vad", "5xif", "5xig", "5xih", "5xii", "5xij", "5xik", "5xil"...

90

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[ "IPR002316" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Megaviricetes", "unclassified sequences" ]

[ 952, 7372, 8411, 14, 269 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 13, 2, 2, 2, 2, 2, 1, 10, 6, 1, 1, 26 ]

12

true

Family

Proline-tRNA ligase, class IIa, archaeal-type

Pro-tRNA-ligase_IIa_arc-type

5

IPR004500

4,500

Prolyl-tRNA synthetase, class IIa, bacterial-type

Pro-tRNA-synth_IIa_bac-type

Family

20,998

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0004827", "GO:0005524", "GO:0006433", "GO:0005737" ]

[ "proline-tRNA ligase activity", "ATP binding", "prolyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "NCBIFAM" ]

[ "TIGR00409" ]

[ "proS_fam_II" ]

[ 20998 ]

1

[ "EC", "GP" ]

[ "6.1.1.15", "GenProp0258" ]

[ "EC:6.1.1.15", "GP:GenProp0258" ]

2

[ "2i4l", "2i4m", "2i4n", "2i4o", "2j3l", "2j3m", "5ucm", "5znj", "5znk", "8w8j", "8w8l", "8w9i" ]

12

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[ "IPR002316" ]

[ "IPR023716", "IPR023717" ]

1

2

0

[ "Bacteria", "Eukaryota", "unclassified Caudoviricetes", "unclassified sequences" ]

[ 19934, 662, 2, 400 ]

4

[ "Escherichia coli (strain K12)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 1, 1 ]

2

true

Family

Prolyl-tRNA synthetase, class IIa, bacterial-type

Pro-tRNA-synth_IIa_bac-type

8

IPR004501

4,501

Phosphotransferase system, EIIC component, type 3

PTS_EIIC_3

Domain

16,708

false

The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS) [ , ] is a major carbohydrate transport system in bacteria. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosp...

[ "GO:0008982", "GO:0009401", "GO:0016020" ]

[ "protein-N(PI)-phosphohistidine-sugar phosphotransferase activity", "phosphoenolpyruvate-dependent sugar phosphotransferase system", "membrane" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "PROFILE", "NCBIFAM" ]

[ "PS51105", "TIGR00410" ]

[ "PTS_EIIC_TYPE_3", "lacE" ]

[ 16702, 13696 ]

2

[ "EC", "GP", "PROSITEDOC" ]

[ "2.7.1.207", "GenProp0119", "PDOC51103" ]

[ "EC:2.7.1.207", "GP:GenProp0119", "PROSITEDOC:PDOC51103" ]

3

[ "3qnq" ]

1

[ "PUB00000073", "PUB00002162", "PUB00003612", "PUB00017027", "PUB00017028", "PUB00017925" ]

[ "2197982", "1537788", "8246840", "7815935", "11361063", "15667312" ]

[ "The bacterial phosphoenolpyruvate: glycose phosphotransferase system.", "Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.", "Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria.", "The bacterial phosp...

[ 1990, 1992, 1993, 1994, 2001, 2005 ]

6

[ "IPR003352" ]

[ "IPR004801" ]

1

0

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 16664, 9, 35 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Domain

Phosphotransferase system, EIIC component, type 3

PTS_EIIC_3

3

IPR004502

4,502

Thioredoxins/glutaredoxin

Thio_glut

Family

69

false

This group of proteins includes thioredoxins, glutaredoxins, protein-disulphide isomerases, amongst others, some of which have several such domains. The sequence of proteins in this group at the redox-active disulphide site, CPYC, matches glutaredoxins rather than thioredoxins, although overall the sequence seems close...

[ "GO:0009055", "GO:0015035", "GO:0045454" ]

[ "electron transfer activity", "protein-disulfide reductase activity", "cell redox homeostasis" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR00411" ]

[ "redox_disulf_1" ]

[ 69 ]

1

[]

0

[ "1fo5", "1nho" ]

2

[]

0

[]

0

null

[ "Methanobacteriota", "bioreactor metagenome" ]

[ 68, 1 ]

2

[]

0

true

Family

Thioredoxins/glutaredoxin

Thio_glut

8

IPR004503

4,503

Serine-tRNA ligase type 2, archaea

Ser-tRNA-ligase_2_arc

Family

119

false

Serine-tRNA ligase ( ) exists as monomer and belongs to class IIa [ ]. The serine-tRNA ligases from a few of the archaea that belong to this group are different from the set of mutually more closely related serine-tRNA ligases from eubacteria, eukaryotes, and other archaea ( ). There are two distinct types of seryl-tRN...

[ "GO:0000166", "GO:0004828", "GO:0005524", "GO:0006434", "GO:0005737" ]

[ "nucleotide binding", "serine-tRNA ligase activity", "ATP binding", "seryl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "HAMAP", "NCBIFAM" ]

[ "MF_01278", "TIGR00415" ]

[ "Ser_tRNA_synth_type2", "serS_MJ" ]

[ 100, 75 ]

2

[ "EC", "GP", "METACYC" ]

[ "6.1.1.11", "GenProp0258", "PWY-6281" ]

[ "EC:6.1.1.11", "GP:GenProp0258", "METACYC:PWY-6281" ]

3

[ "2cim", "2cj9", "2cja", "2cjb", "3w3s" ]

5

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006326", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873", "PUB00088641", "PUB00088642" ]

[ "8364025", "8274143", "1852601", "2053131", "7540217", "10673435", "2203971", "10447505", "10704480", "12458790", "19734148", "15364939" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1995, 2000, 1990, 1999, 2000, 2002, 2009, 2004 ]

12

[]

0

null

[ "Archaea", "unclassified sequences" ]

[ 116, 3 ]

2

[]

0

true

Family

Serine-tRNA ligase type 2, archaea

Ser-tRNA-ligase_2_arc

7

IPR004504

4,504

DNA repair protein RadA

DNA_repair_RadA

Family

24,340

false

RadA/Sms is a highly conserved eubacterial protein that shares sequence similarity with both RecA strand transferase and lon protease. The RadA/Sms family are ATP-dependent proteases involved in both DNA repair and degradation of proteins, peptides, glycopeptides. They are classified in MEROPS peptidase family S16 (lon...

[ "GO:0003684", "GO:0005524", "GO:0006281" ]

[ "damaged DNA binding", "ATP binding", "DNA repair" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_01498", "TIGR00416" ]

[ "RadA_bact", "sms" ]

[ 23191, 24195 ]

2

[ "EC", "METACYC" ]

[ "3.6.4.-", "PWY-7250" ]

[ "EC:3.6.4.-", "METACYC:PWY-7250" ]

2

[ "5lkm", "8rxc" ]

2

[ "PUB00011878", "PUB00100747", "PUB00106485" ]

[ "12446634", "26845522", "28561029" ]

[ "Role for radA/sms in recombination intermediate processing in Escherichia coli.", "Recombinational branch migration by the RadA/Sms paralog of RecA in Escherichia coli.", "Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extension." ]

[ 2002, 2016, 2017 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 23400, 566, 374 ]

3

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 8, 1, 2, 3 ]

4

true

Family

DNA repair protein RadA

DNA_repair_RadA

4

IPR004506

4,506

tRNA-specific 2-thiouridylase MnmA-like

MnmA-like

Family

29,896

false

This family represents tRNA-specific 2-thiouridylase MnmA (sometimes called tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase), which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U) present in the wobble position of some tRNAs [ , ]. This family of enzyme o...

[ "GO:0016740", "GO:0008033" ]

[ "transferase activity", "tRNA processing" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_00144", "TIGR00420", "cd01998" ]

[ "tRNA_thiouridyl_MnmA", "trmU", "MnmA_TRMU-like" ]

[ 27468, 28660, 29879 ]

3

[ "EC", "GP", "GP", "GP", "GP", "METACYC", "METACYC", "REACTOME" ]

[ "2.8.1.13", "GenProp0704", "GenProp1161", "GenProp1313", "GenProp1555", "PWY-7887", "PWY-7892", "R-HSA-6787450" ]

[ "EC:2.8.1.13", "GP:GenProp0704", "GP:GenProp1161", "GP:GenProp1313", "GP:GenProp1555", "METACYC:PWY-7887", "METACYC:PWY-7892", "REACTOME:R-HSA-6787450" ]

8

[ "2der", "2det", "2deu", "2hma" ]

4

[ "PUB00016823", "PUB00017420", "PUB00040232" ]

[ "15165845", "3298234", "16871210" ]

[ "Distinct origins of tRNA(m1G37) methyltransferase.", "Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities.", "Snapshots of tRNA sulphuration via an adenylated intermediate." ]

[ 2004, 1987, 2006 ]

3

[]

0

null

[ "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 26265, 3115, 516 ]

3

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (s...

[ 6, 1, 2, 2, 1, 4, 1, 4, 3, 1, 1, 8 ]

12

true

Family

tRNA-specific 2-thiouridylase MnmA-like

MnmA-like

6

IPR004507

4,507

Flavin prenyltransferase UbiX-like

UbiX-like

Family

16,974

false

In Escherichia coli, the protein UbiX ( ) is a flavin prenyltransferase that has been shown to be involved in the third step of ubiquinone biosynthesis [ ]. It is required for the reaction 3-octaprenyl-4-hydroxybenzoate = 2-octaprenylphenol + CO2 ( ) catalyzed by UbiD and was initially believed to directly catalyse thi...

[]

0

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_01984", "PTHR43374", "TIGR00421" ]

[ "ubiX_pad", "", "ubiX_pad" ]

[ 13990, 12843, 15013 ]

3

[ "EC", "GP" ]

[ "2.5.1.129", "GenProp0136" ]

[ "EC:2.5.1.129", "GP:GenProp0136" ]

2

[ "1sbz", "2ejb", "3zqu", "4rhe", "4rhf", "4zaf", "4zag", "4zal", "4zan", "4zav", "4zaw", "4zax", "4zay", "4zaz", "6m8t", "6m8u", "6m8v", "6qlg", "6qlh", "6qli", "6qlj", "6qlk", "6qll", "6qlv", "7km2", "7km3" ]

26

[ "PUB00009520", "PUB00037596", "PUB00068237", "PUB00068238", "PUB00076706", "PUB00088723" ]

[ "8181743", "15459342", "17889824", "11693915", "26083743", "23645198" ]

[ "PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae.", "Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157: H7.", "The role of UbiX in Escherichia coli coenzyme Q biosynthesis.", "Effect of...

[ 1994, 2004, 2007, 2001, 2015, 2013 ]

6

[]

[ "IPR032901" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 539, 13308, 2903, 224 ]

4

[ "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)" ]

[ 1, 2, 1 ]

3

true

Family

Flavin prenyltransferase UbiX-like

UbiX-like

9

IPR004508

4,508

Thioredoxin-independent 5'-adenylylsulphate reductase

Thioredoxin-indep_APS_Rdtase

Family

1,016

false

This enzyme, involved in the assimilation of inorganic sulphate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenyly...

[ "GO:0016671", "GO:0000103" ]

[ "oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor", "sulfate assimilation" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR00424" ]

[ "APS_reduc" ]

[ 1016 ]

1

[ "EC", "GP", "METACYC" ]

[ "1.8.4.9", "GenProp1392", "PWY-6932" ]

[ "EC:1.8.4.9", "GP:GenProp1392", "METACYC:PWY-6932" ]

3

[]

0

[]

0

[ "IPR004511" ]

[]

1

0

1

[ "Viridiplantae" ]

[ 1016 ]

1

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 15, 2, 9 ]

3

true

Family

Thioredoxin-independent 5'-adenylylsulphate reductase

Thioredoxin-indep_APS_Rdtase

5

IPR004509

4,509

Competence protein ComEA, helix-hairpin-helix domain

Competence_ComEA_HhH

Domain

14,160

false

Competence is the ability of a cell to take up exogenous DNA from its environment, resulting in transformation. It is widespread among bacteria and is probably an important mechanism for the horizontal transfer of genes. DNA usually becomes available by the death and lysis of other cells. Competent bacteria use compone...

[]

0

[ "NCBIFAM" ]

[ "TIGR00426" ]

[ "" ]

[ 14160 ]

1

[ "GP", "REACTOME" ]

[ "GenProp0311", "R-HSA-9029569" ]

[ "GP:GenProp0311", "REACTOME:R-HSA-9029569" ]

2

[ "8dfk", "8dss" ]

2

[ "PUB00052316", "PUB00052317" ]

[ "8901420", "10361283" ]

[ "Who's competent and when: regulation of natural genetic competence in bacteria.", "Mutational analysis of ComS: evidence for the interaction of ComS and MecA in the regulation of competence development in Bacillus subtilis." ]

[ 1996, 1999 ]

2

[ "IPR060575" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Methanothrix harundinacea (strain 6Ac)", "unclassified sequences" ]

[ 13127, 784, 1, 248 ]

4

[ "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 1, 1, 3 ]

4

true

Domain

Competence protein ComEA, helix-hairpin-helix domain

Competence_ComEA_HhH

1

IPR004511

4,511

Phosphoadenosine phosphosulphate/adenosine 5'-phosphosulphate reductase

PAPS/APS_Rdtase

Family

18,990

false

This entry represents a family of phosphoadenosine phosphosulphate (PAPS) reductases and adenosine 5'-phosphosulphate (APS) reductases involved in the assimilatory reduction of inorganic sulphate. The APS reductases can be distinguished from the PAPS reductases by the presence of two additional cysteine pairs thought t...

[ "GO:0004604", "GO:0019379" ]

[ "phosphoadenylyl-sulfate reductase (thioredoxin) activity", "sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin)" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "NCBIFAM", "PIRSF", "NCBIFAM" ]

[ "MF_00063", "NF002537", "PIRSF000857", "TIGR00434" ]

[ "CysH", "PRK02090.1", "PAPS_reductase", "cysH" ]

[ 18687, 18921, 16471, 14927 ]

4

[ "EC", "EC", "GP", "REACTOME" ]

[ "1.8.4", "1.8.4.8", "GenProp1283", "R-MTU-936721" ]

[ "EC:1.8.4", "EC:1.8.4.8", "GP:GenProp1283", "REACTOME:R-MTU-936721" ]

4

[ "1sur", "2goy", "2o8v", "2oq2", "4bwv", "6vpu", "7lhr", "7lhs", "7lhu", "7rge" ]

10

[ "PUB00017739" ]

[ "11940598" ]

[ "The presence of an iron-sulfur cluster in adenosine 5'-phosphosulfate reductase separates organisms utilizing adenosine 5'-phosphosulfate and phosphoadenosine 5'-phosphosulfate for sulfate assimilation." ]

[ 2002 ]

1

[]

[ "IPR004508", "IPR011798", "IPR011800" ]

0

3

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 133, 15784, 2894, 179 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 15, 1, 1, 3, 1, 1, 9 ]

7

true

Family

Phosphoadenosine phosphosulphate/adenosine 5'-phosphosulphate reductase

PAPS/APS_Rdtase

3

IPR004512

4,512

Ribosomal RNA methyltransferase E, gammaproteobacteria

rRNA_MeTrfase_gammaproteobac

Family

1,275

false

The ribosomal RNA large subunit methyltransferase E ( ) methylates the 23S rRNA. It specifically methylates the uridine in position 2552 of 23s rRNA in the 50S particle using S-adenosyl-L-methionine as a substrate. It was previously known as cell division protein ftsJ.

[ "GO:0016436", "GO:0006364" ]

[ "rRNA (uridine) methyltransferase activity", "rRNA processing" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM" ]

[ "TIGR00438" ]

[ "rrmJ" ]

[ 1275 ]

1

[ "EC" ]

[ "2.1.1.166" ]

[ "EC:2.1.1.166" ]

1

[ "1eiz", "1ej0" ]

2

[]

0

[ "IPR015507" ]

[]

1

0

1

[ "Bacteria", "Methanomada group", "Rhodnius prolixus", "bioreactor metagenome" ]

[ 1263, 10, 1, 1 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Ribosomal RNA methyltransferase E, gammaproteobacteria

rRNA_MeTrfase_gammaproteobac

5

IPR004513

4,513

Cell division protein FtsX

FtsX

Family

22,070

false

FtsX is an integral membrane protein encoded in the same operon as signal recognition particle docking protein FtsY and FtsE. FtsE is a hydrophilic nucleotide-binding protein that associates with the inner membrane by means of association with FtsX; FtsE mutants are viable only in high salt, supporting possible roles i...

[ "GO:0051301", "GO:0016020" ]

[ "cell division", "membrane" ]

[ "biological_process", "cellular_component" ]

2

[ "PIRSF", "PANTHER" ]

[ "PIRSF003097", "PTHR47755" ]

[ "FtsX", "" ]

[ 18176, 22070 ]

2

[]

0

[ "4n8n", "4n8o", "6he6", "6hee", "6hfx", "6mk7", "6tpi", "8hd0", "8i6o", "8i6q", "8i6r", "8i6s", "8idb", "8idc", "8idd", "8igq", "8jia", "8tzj", "8tzk", "8tzl", "8w6i", "8w6j", "8x61", "8y3x", "8ymc", "9iue" ]

26

[ "PUB00017427", "PUB00053471", "PUB00059297", "PUB00062360", "PUB00106489", "PUB00106490" ]

[ "10048040", "17307852", "18573177", "16416128", "31376483", "33097670" ]

[ "Molecular characterization of Escherichia coli FtsE and FtsX.", "Interaction between cell division proteins FtsE and FtsZ.", "The FtsEX ABC transporter directs cellular differentiation in Bacillus subtilis.", "Molecular characterisation of ABC transporter type FtsE and FtsX proteins of Mycobacterium tubercul...

[ 1999, 2007, 2008, 2006, 2019, 2020 ]

6

[]

[ "IPR047590", "IPR047929", "IPR058204" ]

0

3

0

[ "Bacteria", "Eukaryota", "Nitrososphaerota", "unclassified Caudoviricetes", "unclassified sequences" ]

[ 21642, 6, 2, 2, 418 ]

5

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Cell division protein FtsX

FtsX

3

IPR004516

4,516

Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit

HisRS/HisZ

Family

46,049

false

This entry represents histidine-tRNA ligase (HisS or HisRS) and its paralogue, ATP phosphoribosyltransferase regulatory subunit (HisZ). Despite the significant sequential and structural similarity, HisRS and HisZ have different functions [ ]. HisRS is a class IIa aminoacyl-tRNA synthetase (ligase), while HisZ is a regu...

[ "GO:0005737" ]

[ "cytoplasm" ]

[ "cellular_component" ]

1

[ "PIRSF", "PANTHER" ]

[ "PIRSF001549", "PTHR43707" ]

[ "His-tRNA_synth", "" ]

[ 43252, 30402 ]

2

[ "EC", "REACTOME", "REACTOME" ]

[ "6.1.1.21", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.21", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

3

[ "1adj", "1ady", "1h4v", "1htt", "1kmm", "1kmn", "1qe0", "1usy", "1wu7", "1z7m", "1z7n", "2el9", "3hri", "3hrk", "3lc0", "3net", "3od1", "3rac", "4e51", "4g84", "4g85", "4phc", "4rdx", "4x5o", "4yp0", "4ypf", "4yrc", "4yre", "4yrf", "4yrg", "4yri", "4yrj"...

54

[ "PUB00037892", "PUB00054292", "PUB00057738", "PUB00060984" ]

[ "15660995", "16051603", "20132829", "10795825" ]

[ "Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit.", "Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog.", "Crystal structures of trypanosomal ...

[ 2005, 2005, 2010, 2000 ]

4

[]

[ "IPR004517", "IPR015807" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 972, 37993, 6196, 17, 871 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 11, 1, 2, 2, 1, 20, 8, 1, 4, 9, 1, 16 ]

12

true

Family

Histidine-tRNA ligase/ATP phosphoribosyltransferase regulatory subunit

HisRS/HisZ

9

IPR004517

4,517

ATP phosphoribosyltransferase regulatory subunit

HisZ

Family

8,855

false

Proteins in this entry are mostly annotated as the ATP phosphoribosyltransferase regulatory subunit (HisZ). However, this entry also includes some histidine-tRNA ligases (HisS or HisRS), which is the paralogue of HisZ. Despite the significant sequential and structural similarity, HisRS and HisZ have different functions...

[ "GO:0000105", "GO:0005737" ]

[ "L-histidine biosynthetic process", "cytoplasm" ]

[ "biological_process", "cellular_component" ]

2

[ "HAMAP", "NCBIFAM" ]

[ "MF_00125", "TIGR00443" ]

[ "HisZ", "hisZ_biosyn_reg" ]

[ 8845, 5837 ]

2

[ "GP" ]

[ "GenProp0109" ]

[ "GP:GenProp0109" ]

1

[ "1usy", "1z7m", "1z7n", "3od1", "5m8h", "6ftt", "6fu2", "6fu7", "6fua", "6r02", "7z6r", "8oy0" ]

12

[ "PUB00037892", "PUB00054292", "PUB00057738", "PUB00060984" ]

[ "15660995", "16051603", "20132829", "10795825" ]

[ "Regulation of the hetero-octameric ATP phosphoribosyl transferase complex from Thermotoga maritima by a tRNA synthetase-like subunit.", "Activation of the hetero-octameric ATP phosphoribosyl transferase through subunit interface rearrangement by a tRNA synthetase paralog.", "Crystal structures of trypanosomal ...

[ 2005, 2005, 2010, 2000 ]

4

[ "IPR004516" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 372, 8388, 7, 88 ]

4

[]

0

true

Family

ATP phosphoribosyltransferase regulatory subunit

HisZ

5

IPR004518

4,518

NTP pyrophosphohydrolase MazG-like domain

MazG-like_dom

Domain

31,285

false

This domain is found in a group of prokaryotic proteins which includes Escherichia coli MazG, which hydrolyses all canonical nucleoside triphosphates but it also might have a 'housecleaning' function by hydrolysing noncanonical NTPs, whose incorporation into the nascent DNA leads to the increased mutagenesis and DNA da...

[]

0

[ "PFAM" ]

[ "PF03819" ]

[ "MazG" ]

[ 31285 ]

1

[]

0

[ "1vmg", "2gta", "2p06", "2q5z", "2q73", "2q9l", "2yxh", "3cra", "3crc", "5ie9", "7yh5" ]

11

[ "PUB00013554", "PUB00014610", "PUB00051103", "PUB00078110", "PUB00078111", "PUB00079704" ]

[ "12657645", "12218018", "18353782", "16390452", "20529853", "15740738" ]

[ "Thermotoga maritima MazG protein has both nucleoside triphosphate pyrophosphohydrolase and pyrophosphatase activities.", "MazG, a nucleoside triphosphate pyrophosphohydrolase, interacts with Era, an essential GTPase in Escherichia coli.", "Crystal structure of Escherichia coli MazG, the regulator of nutritiona...

[ 2003, 2002, 2008, 2006, 2010, 2005 ]

6

[]

[ "IPR044548", "IPR048011", "IPR048015" ]

0

3

0

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 460, 28920, 668, 518, 719 ]

5

[ "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 1, 2, 1 ]

3

true

Domain

NTP pyrophosphohydrolase MazG-like domain

MazG-like_dom

9

IPR004519

4,519

DNA-directed RNA polymerase, subunit E/RPC8

RNAP_E/RPC8

Family

2,266

false

This family includes RNA polymerase III subunit RPC8, and archaeal DNA-directed RNA polymerase subunit Rpo7 (previously known as RNA polymerase subunits RpoE and RpoE1). These RNA polymerases catalyse the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. In humans, RPC8 is an spec...

[ "GO:0003677", "GO:0003899", "GO:0006351" ]

[ "DNA binding", "DNA-directed RNA polymerase activity", "DNA-templated transcription" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR00448" ]

[ "rpoE" ]

[ 2266 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-HSA-1834949", "R-HSA-73780", "R-HSA-73980", "R-HSA-749476", "R-HSA-76061", "R-HSA-76066", "R-HSA-76071", "R-MMU-76061", "R-MMU-76066", "R-MMU-76071", "R-SCE-76066", "R-SPO-76061", "R-SPO-76066" ]

[ "REACTOME:R-HSA-1834949", "REACTOME:R-HSA-73780", "REACTOME:R-HSA-73980", "REACTOME:R-HSA-749476", "REACTOME:R-HSA-76061", "REACTOME:R-HSA-76066", "REACTOME:R-HSA-76071", "REACTOME:R-MMU-76061", "REACTOME:R-MMU-76066", "REACTOME:R-MMU-76071", "REACTOME:R-SCE-76066", "REACTOME:R-SPO-76061", "...

13

[ "1go3", "2ckz", "2pmz", "2waq", "2wb1", "2y0s", "3ayh", "3hkz", "4ayb", "4qiw", "4qjf", "4v8s", "5fj8", "5fj9", "5fja", "6cnb", "6cnc", "6cnd", "6cnf", "6eu0", "6eu1", "6eu2", "6eu3", "6f40", "6f41", "6f42", "6f44", "6kf3", "6kf4", "6kf9", "6tut", "7a6h"...

79

[ "PUB00000061", "PUB00033173", "PUB00060118", "PUB00099660", "PUB00099662", "PUB00099663", "PUB00099664", "PUB00099665" ]

[ "3052291", "10499798", "19631370", "19609254", "33335104", "33558764", "25311937", "33558766" ]

[ "Structure and function of bacterial sigma factors.", "Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution.", "RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway.", "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA...

[ 1988, 1999, 2009, 2009, 2020, 2021, 2014, 2021 ]

8

[ "IPR045113" ]

[ "IPR046399" ]

1

0

[ "Archaea", "Eiseniibacteriota bacterium", "Eukaryota", "unclassified sequences" ]

[ 889, 1, 1337, 39 ]

4

[ "Danio rerio", "Homo sapiens", "Mus musculus", "Rattus norvegicus", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 1, 1, 2, 2, 1, 1 ]

6

true

Family

DNA-directed RNA polymerase, subunit E/RPC8

RNAP_E/RPC8

7

IPR004522

4,522

Asparagine-tRNA ligase

Asn-tRNA-ligase

Family

21,117

false

Asparagine tRNA ligase ( ) is an alpha2 dimer that belongs to class IIb. There is a striking similarity between asparagine-tRNA ligases and archaeal/eukaryotic type aspartyl-tRNA ligases ( ) and a striking divergence of bacterial type aspartyl-tRNA ligases ( ). This family, AsnS, represents asparagine-tRNA ligases from...

[ "GO:0000166", "GO:0004816", "GO:0005524", "GO:0006421" ]

[ "nucleotide binding", "asparagine-tRNA ligase activity", "ATP binding", "asparaginyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_00534", "TIGR00457" ]

[ "Asn_tRNA_synth", "asnS" ]

[ 14083, 21037 ]

2

[ "EC", "GP", "GP", "REACTOME", "REACTOME" ]

[ "6.1.1.22", "GenProp0258", "GenProp0259", "R-HSA-379716", "R-HSA-379726" ]

[ "EC:6.1.1.22", "GP:GenProp0258", "GP:GenProp0259", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-379726" ]

5

[ "1x54", "1x55", "1x56", "2xgt", "2xti", "3m4p", "3m4q", "5xix", "5zg8", "6pqh", "8h53", "8tc7", "8tc8", "8tc9", "9sh8", "9sh9" ]

16

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 2000, 1990, 1999, 2000, 2002 ]

9

[ "IPR002312" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 175, 12146, 8640, 24, 132 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 17, 1, 3, 2, 1, 7, 6, 2, 7, 13, 2, 2, 14 ]

13

true

Family

Asparagine-tRNA ligase

Asn-tRNA-ligase

3

IPR004523

4,523

Aspartate-tRNA synthetase, type 2

Asp-tRNA_synthase_2

Family

11,226

false

Aspartyl tRNA synthetase is an alpha2 dimer that belongs to class IIb. Structural analysis combined with mutagenesis and enzymology data on the yeast enzyme point to a tRNA binding process that starts by a recognition event between the tRNA anticodon loop and the synthetase anticodon binding module [ ]. This family rep...

[ "GO:0000166", "GO:0004815", "GO:0005524", "GO:0006422", "GO:0005737" ]

[ "nucleotide binding", "aspartate-tRNA ligase activity", "ATP binding", "aspartyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_02075", "PTHR43450", "TIGR00458" ]

[ "Asp_tRNA_synth_type2", "", "aspS_nondisc" ]

[ 9030, 11178, 7891 ]

3

[ "EC", "GP", "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1", "GenProp0258", "GenProp1660", "R-DDI-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-9856649", "R-MMU-9856649", "R-RNO-9856649" ]

[ "EC:6.1.1", "GP:GenProp0258", "GP:GenProp1660", "REACTOME:R-DDI-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649", "REACTOME:R-RNO-9856649" ]

9

[ "1asy", "1asz", "1b8a", "1eov", "1n9w", "1wyd", "3i7f", "3kfu", "3nel", "3nem", "3nen", "4j15", "5y6l", "6iy6", "6od8", "9m5m", "9m5n", "9m5o", "9npj" ]

19

[ "PUB00006538" ]

[ "10873455" ]

[ "The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain." ]

[ 2000 ]

1

[ "IPR002312" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Viruses", "metagenomes" ]

[ 988, 2680, 7430, 12, 116 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 8, 1, 1, 2, 8, 5, 2, 6, 3, 1, 1, 13 ]

12

true

Family

Aspartate-tRNA synthetase, type 2

Asp-tRNA_synthase_2

2

IPR004524

4,524

Aspartate-tRNA ligase, type 1

Asp-tRNA-ligase_1

Family

30,439

false

Aspartate tRNA ligase (also known as Aspartyl-tRNA synthetase, AspRS) is an alpha2 dimer that belongs to class IIb. Structural analysis combined with mutagenesis and enzymology data on the yeast enzyme point to a tRNA binding process that starts by a recognition event between the tRNA anticodon loop and the ligase anti...

[ "GO:0005524", "GO:0016874" ]

[ "ATP binding", "ligase activity" ]

[ "molecular_function", "molecular_function" ]

2

[ "HAMAP", "NCBIFAM", "NCBIFAM" ]

[ "MF_00044", "NF001750", "TIGR00459" ]

[ "Asp_tRNA_synth_type1", "PRK00476.1", "aspS_bact" ]

[ 29586, 28869, 29804 ]

3

[ "EC", "GP", "REACTOME" ]

[ "6.1.1", "GenProp0258", "R-HSA-379726" ]

[ "EC:6.1.1", "GP:GenProp0258", "REACTOME:R-HSA-379726" ]

3

[ "1c0a", "1efw", "1eqr", "1g51", "1il2", "1l0w", "4ah6", "4o2d", "4rmf", "4wj3", "4wj4", "5w25", "6hhv", "6hhw", "6hhx", "6sjc", "6wom", "7ap4" ]

18

[ "PUB00006538" ]

[ "10873455" ]

[ "The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain." ]

[ 2000 ]

1

[ "IPR002312" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "Microviridae sp. ctRQq14", "unclassified sequences" ]

[ 20, 25624, 4316, 1, 478 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 6, 1, 1, 2, 1, 9, 2, 1, 5, 5, 1, 1, 6 ]

13

true

Family

Aspartate-tRNA ligase, type 1

Asp-tRNA-ligase_1

7

IPR004525

4,525

Elongation factor P--(R)-beta-lysine ligase

EpmA

Family

5,940

false

This entry represents the elongation factor P--(R)-beta-lysine ligase (also known as EpmA). Together with EpmB, it is involved in the beta-lysylation step of the post-translational modification of translation elongation factor P (EF-P) [ ]. It catalyses the ATP-dependent activation of (R)-beta-lysine produced by EpmB, ...

[ "GO:0004824", "GO:0005524", "GO:0006430", "GO:0005737" ]

[ "lysine-tRNA ligase activity", "ATP binding", "lysyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_00174", "TIGR00462" ]

[ "EF_P_modif_A", "genX" ]

[ 1765, 5940 ]

2

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "METACYC", "...

[ "6.3.2.-", "GenProp0988", "PWY-6289", "PWY-6374", "PWY-6378", "PWY-6379", "PWY-6409", "PWY-6574", "PWY-7510", "PWY-7533", "PWY-7542", "PWY-7543", "PWY-7549", "PWY-7555", "PWY-7556", "PWY-7561", "PWY-7563", "PWY-7565", "PWY-7569", "PWY-7570", "PWY-7571", "PWY-7577", "PWY-7...

[ "EC:6.3.2.-", "GP:GenProp0988", "METACYC:PWY-6289", "METACYC:PWY-6374", "METACYC:PWY-6378", "METACYC:PWY-6379", "METACYC:PWY-6409", "METACYC:PWY-6574", "METACYC:PWY-7510", "METACYC:PWY-7533", "METACYC:PWY-7542", "METACYC:PWY-7543", "METACYC:PWY-7549", "METACYC:PWY-7555", "METACYC:PWY-755...

43

[ "3a5y", "3a5z", "3g1z" ]

3

[ "PUB00064725", "PUB00064726" ]

[ "20670890", "9826331" ]

[ "PoxA, yjeK, and elongation factor P coordinately modulate virulence and drug resistance in Salmonella enterica.", "Molecular and functional characterization of Salmonella enterica serovar typhimurium poxA gene: effect on attenuation of virulence and protection." ]

[ 2010, 1998 ]

2

[]

0

null

[ "Bacteria", "Opisthokonta", "unclassified sequences" ]

[ 5871, 5, 64 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Elongation factor P--(R)-beta-lysine ligase

EpmA

5

IPR004526

4,526

Glutamyl-tRNA synthetase, archaeal/eukaryotic cytosolic

Glu-tRNA-synth_arc/euk

Family

6,038

false

This entry are mostly eukaryotic cytosolic and archaeal forms of the glutamyl-tRNA synthetase. The glutamyl-tRNA synthetases of the eukaryotic cytosol and of the Archaea are more similar to glutaminyl-tRNA synthetases than to bacterial glutamyl-tRNA synthetases. In many species, the charging of tRNA (gln) proceeds firs...

[ "GO:0000166", "GO:0004818", "GO:0005524", "GO:0006424", "GO:0005737" ]

[ "nucleotide binding", "glutamate-tRNA ligase activity", "ATP binding", "glutamyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "HAMAP", "NCBIFAM" ]

[ "MF_02076", "TIGR00463" ]

[ "Glu_tRNA_synth_type2", "gltX_arch" ]

[ 5269, 6026 ]

2

[ "EC", "GP", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "6.1.1.17", "GenProp0217", "GenProp0258", "PWY-5188", "R-DME-9856649", "R-HSA-2408522", "R-HSA-379716", "R-HSA-6782315", "R-HSA-9856649", "R-MMU-9856649" ]

[ "EC:6.1.1.17", "GP:GenProp0217", "GP:GenProp0258", "METACYC:PWY-5188", "REACTOME:R-DME-9856649", "REACTOME:R-HSA-2408522", "REACTOME:R-HSA-379716", "REACTOME:R-HSA-6782315", "REACTOME:R-HSA-9856649", "REACTOME:R-MMU-9856649" ]

10

[ "3aii", "7wai", "7waj", "7wak", "7wal", "7wao", "7wrs", "7wru" ]

8

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006397", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873", "PUB00103850", "PUB00103851" ]

[ "8364025", "8274143", "1852601", "2053131", "9426192", "10673435", "2203971", "10447505", "10704480", "12458790", "9746349", "8078941" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1997, 2000, 1990, 1999, 2000, 2002, 1998, 1994 ]

12

[ "IPR000924" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 933, 40, 5043, 22 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 5, 1, 2, 1, 6, 2, 1, 4, 4, 1, 1, 9 ]

12

true

Family

Glutamyl-tRNA synthetase, archaeal/eukaryotic cytosolic

Glu-tRNA-synth_arc/euk

2

IPR004527

4,527

Glutamate-tRNA ligase, bacterial/mitochondrial

Glu-tRNA-ligase_bac/mito

Family

34,248

false

This entry contains nondiscriminating glutamyl-tRNA synthetase EARS2, which is found in mitochondria [ ]. Glutamate-tRNA ligase (also known as glutamyl-tRNA synthetase; ) is a class I aminoacyl-tRNA synthetase. This enzyme shares similarities with glutaminyl-tRNA synthetase in terms of structure and catalytic propertie...

[ "GO:0000166", "GO:0004818", "GO:0005524", "GO:0006424" ]

[ "nucleotide binding", "glutamate-tRNA ligase activity", "ATP binding", "glutamyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_00022", "TIGR00464" ]

[ "Glu_tRNA_synth_type1", "gltX_bact" ]

[ 33331, 33642 ]

2

[ "EC", "GP", "GP", "GP", "GP", "METACYC", "REACTOME" ]

[ "6.1.1.17", "GenProp0217", "GenProp0258", "GenProp1383", "GenProp1701", "PWY-5188", "R-HSA-379726" ]

[ "EC:6.1.1.17", "GP:GenProp0217", "GP:GenProp0258", "GP:GenProp1383", "GP:GenProp1701", "METACYC:PWY-5188", "REACTOME:R-HSA-379726" ]

7

[ "1g59", "1gln", "1j09", "1n75", "1n77", "1n78", "2cfo", "2cuz", "2cv0", "2cv1", "2cv2", "2dxi", "2ja2", "2o5r", "3afh", "3akz", "3al0", "3pnv", "3pny", "4g6z", "4gri", "5h4v", "5tgt", "6b1p", "6b1z", "6brl", "7k86", "8i9i", "8jpv", "8vc5", "9y81", "9ymm"...

32

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006397", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873", "PUB00103850", "PUB00103851", "PUB00153138" ]

[ "8364025", "8274143", "1852601", "2053131", "9426192", "10673435", "2203971", "10447505", "10704480", "12458790", "9746349", "8078941", "19805282" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1997, 2000, 1990, 1999, 2000, 2002, 1998, 1994, 2009 ]

13

[ "IPR049940" ]

[]

1

0

1

[ "Bacteria", "Candidatus Methanofastidiosum methylothiophilum", "Eukaryota", "Viruses", "unclassified sequences" ]

[ 29569, 1, 4143, 2, 533 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 3, 1, 7, 3, 1, 2, 2, 1, 2, 3, 1, 1, 11 ]

13

true

Family

Glutamate-tRNA ligase, bacterial/mitochondrial

Glu-tRNA-ligase_bac/mito

4

IPR004528

4,528

3-deoxy-D-manno-octulosonate cytidylyltransferase

KdsB

Family

15,213

false

3-Deoxy-D-manno-octulosonate cytidylyltransferase ( ) activates KDO, a required 8-carbon sugar, for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. It acts as a homodimer and catalyses the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate and pyrophospha...

[ "GO:0008690" ]

[ "3-deoxy-manno-octulosonate cytidylyltransferase activity" ]

[ "molecular_function" ]

1

[ "HAMAP", "NCBIFAM", "CDD" ]

[ "MF_00057", "TIGR00466", "cd02517" ]

[ "KdsB", "kdsB", "CMP-KDO-Synthetase" ]

[ 12334, 13776, 15109 ]

3

[ "EC", "GP", "GP", "GP", "METACYC" ]

[ "2.7.7.38", "GenProp0204", "GenProp1325", "GenProp1647", "PWY-1269" ]

[ "EC:2.7.7.38", "GP:GenProp0204", "GP:GenProp1325", "GP:GenProp1647", "METACYC:PWY-1269" ]

5

[ "1gq9", "1gqc", "1h6j", "1h7e", "1h7f", "1h7g", "1h7h", "1h7t", "1vh1", "1vh3", "1vic", "2y6p", "3duv", "3jtj", "3k8d", "3k8e", "3oam", "3pol", "3tqd", "4fcu", "4xwi", "8ees" ]

22

[ "PUB00025543", "PUB00080738", "PUB00080739", "PUB00082311" ]

[ "8706906", "12499564", "3681901", "23413030" ]

[ "The three-dimensional structure of capsule-specific CMP: 2-keto-3-deoxy-manno-octonic acid synthetase from Escherichia coli.", "Crystallization and preliminary X-ray crystallographic studies of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae.", "Design and synthesis of peptide deriv...

[ 1996, 2003, 1987, 2013 ]

4

[ "IPR003329" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Fadolivirus FV1/VV64", "Methanobacteriati", "unclassified sequences" ]

[ 14117, 811, 1, 20, 264 ]

5

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 1, 2, 4 ]

4

true

Family

3-deoxy-D-manno-octulosonate cytidylyltransferase

KdsB

3

IPR004529

4,529

Phenylalanyl-tRNA synthetase, class IIc, alpha subunit

Phe-tRNA-synth_IIc_asu

Family

29,835

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000166", "GO:0004826", "GO:0005524", "GO:0006432", "GO:0005737" ]

[ "nucleotide binding", "phenylalanine-tRNA ligase activity", "ATP binding", "phenylalanyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR00468" ]

[ "pheS" ]

[ 29835 ]

1

[ "EC", "GP", "REACTOME" ]

[ "6.1.1.20", "GenProp0258", "R-HSA-379716" ]

[ "EC:6.1.1.20", "GP:GenProp0258", "REACTOME:R-HSA-379716" ]

3

[ "1b70", "1b7y", "1eiy", "1jjc", "1pys", "2akw", "2aly", "2amc", "2iy5", "2rhq", "2rhs", "3hfz", "3l4g", "3pco", "3teh", "4p71", "4p72", "4p73", "4p74", "4p75", "4tva", "6oz5", "6p24", "6p26", "6p8t", "7by6", "7daw", "7db7", "7db8", "7dpi", "7k98", "7k9m"...

41

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006305", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "8199244", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1993, 2000, 1990, 1999, 2000, 2002 ]

10

[]

[ "IPR022911", "IPR022917" ]

0

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ctBLh2", "unclassified sequences" ]

[ 937, 24191, 4210, 1, 496 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 4, 2, 1, 1, 1, 4, 2, 1, 5, 5, 1, 1, 5 ]

13

true

Family

Phenylalanyl-tRNA synthetase, class IIc, alpha subunit

Phe-tRNA-synth_IIc_asu

3

IPR004530

4,530

Phenylalanyl-tRNA synthetase, class IIc, mitochondrial

Phe-tRNA-synth_IIc_mito

Family

3,397

false

Phenylalanyl-tRNA synthetase ( ) is an alpha2/beta2 tetramer composed of 2 subunits that belongs to class IIc. In eubacteria, a small subunit (pheS gene) can be designated as beta (E. coli) or alpha subunit (nomenclature adopted in InterPro). Reciprocally the large subunit (pheT gene) can be designated as alpha (E. col...

[ "GO:0000166", "GO:0004826", "GO:0005524", "GO:0006432", "GO:0005737" ]

[ "nucleotide binding", "phenylalanine-tRNA ligase activity", "ATP binding", "phenylalanyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR00469" ]

[ "pheS_mito" ]

[ 3397 ]

1

[ "EC", "REACTOME" ]

[ "6.1.1.20", "R-HSA-379726" ]

[ "EC:6.1.1.20", "REACTOME:R-HSA-379726" ]

2

[ "3cmq", "3hfv", "3teg", "3tup", "5mgh", "5mgu", "5mgv", "5mgw", "8p8x" ]

9

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006305", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "8199244", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1993, 2000, 1990, 1999, 2000, 2002 ]

10

[]

0

null

[ "Eukaryota" ]

[ 3397 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 3, 2, 1, 1, 1, 2, 1, 2, 4, 1, 1, 12 ]

12

true

Family

Phenylalanyl-tRNA synthetase, class IIc, mitochondrial

Phe-tRNA-synth_IIc_mito

9

IPR004531

4,531

Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archaeal/eukaryotic type

Phe-tRNA-synth_IIc_bsu_arc_euk

Family

5,926

false

Aminoacyl-tRNA synthetases (also known as aminoacyl-tRNA ligases) catalyse the attachment of amino acids to their cognate transfer RNA molecules through a highly specific two-step reaction [ , ]. These enzymes vary widely in size and oligomeric state, and share limited sequence homology [ ]. The 20 aminoacyl-tRNA synth...

[ "GO:0000166", "GO:0004826", "GO:0005524", "GO:0006432", "GO:0005737" ]

[ "nucleotide binding", "phenylalanine-tRNA ligase activity", "ATP binding", "phenylalanyl-tRNA aminoacylation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR00471" ]

[ "pheT_arch" ]

[ 5926 ]

1

[ "EC", "GP", "REACTOME" ]

[ "6.1.1.20", "GenProp0258", "R-HSA-379716" ]

[ "EC:6.1.1.20", "GP:GenProp0258", "REACTOME:R-HSA-379716" ]

3

[ "2cxi", "3l4g", "7by6", "7dpi", "8s8b" ]

5

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006305", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "8199244", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1993, 2000, 1990, 1999, 2000, 2002 ]

10

[ "IPR045060" ]

[ "IPR022918" ]

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 927, 164, 4808, 27 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 4, 1, 2, 1, 4, 7, 1, 3, 3, 1, 1, 8 ]

12

true

Family

Phenylalanyl-tRNA synthetase, class IIc, beta subunit, archaeal/eukaryotic type

Phe-tRNA-synth_IIc_bsu_arc_euk

1

IPR004532

4,532

Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type

Phe-tRNA-ligase_IIc_bsu_bact

Family

26,743

false

Phenylalanine-tRNA ligase ( ) is an alpha2/beta2 tetramer composed of 2 subunits that belongs to class IIc. In eubacteria, a small subunit (pheS gene) can be designated as beta (E. coli) or alpha subunit (see ). Reciprocally the large subunit (pheT gene) can be designated as alpha (E. coli) or beta. In all other kingdo...

[ "GO:0000287", "GO:0004826", "GO:0005524", "GO:0006432" ]

[ "magnesium ion binding", "phenylalanine-tRNA ligase activity", "ATP binding", "phenylalanyl-tRNA aminoacylation" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process" ]

4

[ "HAMAP", "NCBIFAM" ]

[ "MF_00283", "TIGR00472" ]

[ "Phe_tRNA_synth_beta1", "pheT_bact" ]

[ 26379, 26404 ]

2

[ "EC", "GP" ]

[ "6.1.1.20", "GenProp0258" ]

[ "EC:6.1.1.20", "GP:GenProp0258" ]

2

[ "1b70", "1b7y", "1eiy", "1jjc", "1pys", "2akw", "2aly", "2amc", "2iy5", "2rhq", "2rhs", "3hfz", "3pco", "3teh", "4p71", "4p72", "4p73", "4p74", "4p75", "4tva", "6oz5", "6p24", "6p26", "6p8t", "7daw", "7db7", "7db8", "7k98", "7k9m", "7ka0", "7kab", "7n8y"...

37

[ "PUB00000386", "PUB00000723", "PUB00004391", "PUB00005365", "PUB00006305", "PUB00006477", "PUB00007191", "PUB00007363", "PUB00079872", "PUB00079873" ]

[ "8364025", "8274143", "1852601", "2053131", "8199244", "10673435", "2203971", "10447505", "10704480", "12458790" ]

[ "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.", "The aminoacyl-tRNA synthetase family: modules at work.", "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.", "Classes of aminoacyl-tRNA synthetases and the establ...

[ 1993, 1993, 1991, 1991, 1993, 2000, 1990, 1999, 2000, 2002 ]

10

[ "IPR045060" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 2, 26165, 122, 454 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Phenylalanine-tRNA ligase, class IIc, beta subunit, bacterial type

Phe-tRNA-ligase_IIc_bsu_bact

1

IPR004533

4,533

CDP-diacylglycerol--serine O-phosphatidyltransferase

CDP-diaglyc--ser_O-PTrfase

Family

13,383

false

This enzyme, CDP-diacylglycerol--serine O-phosphatidyltransferase, is involved in phospholipid biosynthesis catalyzing the reaction CDP-diacylglycerol + L-serine = CMP + L-1-phosphatidylserine. Members of this family do not bear any significant sequence similarity to the corresponding Escherichia coli protein.

[]

0

[ "NCBIFAM" ]

[ "TIGR00473" ]

[ "pssA" ]

[ 13383 ]

1

[ "EC", "METACYC" ]

[ "2.7.8.8", "PWY-5669" ]

[ "EC:2.7.8.8", "METACYC:PWY-5669" ]

2

[ "7b1k", "7b1l", "7b1n", "7pow" ]

4

[]

0

[ "IPR000462" ]

[ "IPR016271", "IPR026475" ]

1

2

0

[ "Archaea", "Bacteria", "Eukaryota", "Siphoviridae sp. ct6rT12", "unclassified sequences" ]

[ 160, 11533, 1521, 1, 168 ]

5

[ "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 1, 1, 1 ]

3

true

Family

CDP-diacylglycerol--serine O-phosphatidyltransferase

CDP-diaglyc--ser_O-PTrfase

1

IPR004534

4,534

L-seryl-tRNA(Sec) selenium transferase

SelA_trans

Family

7,243

false

In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-pri...

[ "GO:0004125", "GO:0001514", "GO:0005737" ]

[ "L-seryl-tRNA(Sec) selenium transferase activity", "selenocysteine incorporation", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00423", "TIGR00474" ]

[ "SelA", "selA" ]

[ 7243, 7039 ]

2

[ "EC", "GP" ]

[ "2.9.1.1", "GenProp1499" ]

[ "EC:2.9.1.1", "GP:GenProp1499" ]

2

[ "3w1h", "3w1i", "3w1j", "3w1k", "3wcn", "3wco", "8uzw" ]

7

[ "PUB00045615" ]

[ "17937620" ]

[ "Towards understanding selenocysteine incorporation into bacterial proteins." ]

[ 2007 ]

1

[]

0

null

[ "Bacteria", "Eukaryota", "metagenomes" ]

[ 7043, 31, 169 ]

3

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

L-seryl-tRNA(Sec) selenium transferase

SelA_trans

1

IPR004535

4,535

Translation elongation factor, selenocysteine-specific

Transl_elong_SelB

Family

6,670

false

In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or...

[ "GO:0003723", "GO:0003746", "GO:0005525", "GO:0001514", "GO:0005737" ]

[ "RNA binding", "translation elongation factor activity", "GTP binding", "selenocysteine incorporation", "cytoplasm" ]

[ "molecular_function", "molecular_function", "molecular_function", "biological_process", "cellular_component" ]

5

[ "NCBIFAM" ]

[ "TIGR00475" ]

[ "selB" ]

[ 6670 ]

1

[]

0

[ "4ac9", "4aca", "4acb", "4zu9", "5lzb", "5lzc", "5lzd" ]

7

[ "PUB00033963" ]

[ "15665870" ]

[ "Structural basis for mRNA recognition by elongation factor SelB." ]

[ 2005 ]

1

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 42, 6496, 14, 118 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Translation elongation factor, selenocysteine-specific

Transl_elong_SelB

1

IPR004536

4,536

Selenophosphate synthetase

SPS/SelD

Family

14,119

false

The UGA (TGA) codon is normally a termination codon, however it is also used as a selenocysteine (Sec) codon by numerous organisms [ ]. Sec is the 21st amino acid that is inserted into selenoproteins (protein that includes a selenocysteine (Se-Cys) amino acid residue). The synthesis of Sec and its incorporation into pr...

[ "GO:0005524" ]

[ "ATP binding" ]

[ "molecular_function" ]

1

[ "PIRSF", "PANTHER", "NCBIFAM", "CDD" ]

[ "PIRSF036407", "PTHR10256", "TIGR00476", "cd02195" ]

[ "Selenphspht_syn", "", "selD", "SelD" ]

[ 11660, 13883, 13457, 12564 ]

4

[ "EC", "GP", "GP", "GP", "METACYC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "2.7.9.3", "GenProp0692", "GenProp0726", "GenProp1499", "PWY-6281", "R-CEL-2408557", "R-DDI-2408557", "R-DME-2408557", "R-DRE-2408557", "R-HSA-2408557", "R-MMU-2408557", "R-SSC-2408557" ]

[ "EC:2.7.9.3", "GP:GenProp0692", "GP:GenProp0726", "GP:GenProp1499", "METACYC:PWY-6281", "REACTOME:R-CEL-2408557", "REACTOME:R-DDI-2408557", "REACTOME:R-DME-2408557", "REACTOME:R-DRE-2408557", "REACTOME:R-HSA-2408557", "REACTOME:R-MMU-2408557", "REACTOME:R-SSC-2408557" ]

12

[ "2yye", "2zau", "2zod", "3fd5", "3fd6", "3u0o", "5l16", "9hjt", "9hju" ]

9

[ "PUB00000070", "PUB00014690", "PUB00014691", "PUB00072493", "PUB00072494", "PUB00072496", "PUB00072497" ]

[ "2142875", "9398525", "8986768", "8811175", "2405383", "15534230", "11258485" ]

[ "Selenium biochemistry.", "SelD homolog from Drosophila lacking selenide-dependent monoselenophosphate synthetase activity.", "Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism?", "Selenocysteine.", "In vitro synt...

[ 1990, 1997, 1996, 1996, 1990, 2004, 2000 ]

7

[]

[ "IPR023061" ]

0

1

0

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 79, 10548, 3229, 263 ]

4

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Rattus norvegicus" ]

[ 1, 3, 5, 1, 8, 6, 6 ]

7

true

Family

Selenophosphate synthetase

SPS/SelD

5

IPR004537

4,537

Tellurite resistance methyltransferase, TehB

Tellurite-R_MeTrfase_TehB

Family

2,159

false

Tellurite resistance protein TehB is part of a tellurite-reducing operon tehA and tehB. When present in high copy number, TehB is responsible for potassium tellurite resistance, probably by increasing the reduction rate of tellurite to metallic tellurium within the bacterium. TehB is a cytoplasmic protein which possess...

[ "GO:0008757", "GO:0046690", "GO:0005737" ]

[ "S-adenosylmethionine-dependent methyltransferase activity", "response to tellurium ion", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "NCBIFAM" ]

[ "TIGR00477" ]

[ "tehB" ]

[ 2159 ]

1

[]

0

[ "2i6g", "2xva", "2xvm", "3m70", "4dq0" ]

5

[ "PUB00014885" ]

[ "11053398" ]

[ "Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance." ]

[ 2000 ]

1

[]

[ "IPR014431" ]

0

1

0

[ "Bacteria", "Eukaryota" ]

[ 2154, 5 ]

2

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Tellurite resistance methyltransferase, TehB

Tellurite-R_MeTrfase_TehB

2

IPR004538

4,538

Hemolysin A /rRNA methyltransferase TlyA

Hemolysin_A/TlyA

Family

14,983

false

Haemolysins are exotoxins that attack blood cell membranes and cause cell rupture. The mechanism of action is not well defined. Hemolysin A is induced by sodium ribonucleate, and is produced by pathogenic bacterial strains. Haemolysin A from Treponema hyodysenteriae causes swine dysentery [ ]. The homologous protein fr...

[]

0

[ "PIRSF", "NCBIFAM" ]

[ "PIRSF005578", "TIGR00478" ]

[ "TlyA", "tly" ]

[ 13969, 13456 ]

2

[]

0

[ "3hp7", "3opn", "5ks2", "5kyg", "7s0s" ]

5

[ "PUB00043014", "PUB00043015", "PUB00059301", "PUB00059302" ]

[ "1730486", "9611795", "20854656", "21443791" ]

[ "Cloning and expression of a Serpula (Treponema) hyodysenteriae hemolysin gene.", "Characterization of a haemolysin from Mycobacterium tuberculosis with homology to a virulence factor of Serpulina hyodysenteriae.", "Molecular characterization of tlyA gene product, Rv1694 of Mycobacterium tuberculosis: a non-con...

[ 1992, 1998, 2010, 2011 ]

4

[ "IPR047048" ]

[]

1

0

1

[ "Bacteria", "Eukaryota", "Methanobacteriota", "unclassified sequences" ]

[ 14064, 618, 7, 294 ]

4

[ "Arabidopsis thaliana", "Oryza sativa subsp. japonica", "Zea mays" ]

[ 4, 3, 2 ]

3

true

Family

Hemolysin A /rRNA methyltransferase TlyA

Hemolysin_A/TlyA

9

IPR004539

4,539

Translation elongation factor EF1A, eukaryotic/archaeal

Transl_elong_EF1A_euk/arc

Family

24,661

false

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ , , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the pept...

[ "GO:0003746", "GO:0005525", "GO:0006414" ]

[ "translation elongation factor activity", "GTP binding", "translational elongation" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00118_A", "TIGR00483" ]

[ "EF_Tu_A", "EF-1_alpha" ]

[ 7997, 24654 ]

2

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOM...

[ "R-BTA-156842", "R-BTA-3371511", "R-BTA-6798695", "R-BTA-8876725", "R-CEL-3371511", "R-CEL-6798695", "R-CEL-8876725", "R-DDI-156842", "R-DDI-3371511", "R-DDI-6798695", "R-DDI-8876725", "R-DME-156842", "R-DME-3371511", "R-DME-6798695", "R-DME-8876725", "R-GGA-3371511", "R-GGA-6798695"...

[ "REACTOME:R-BTA-156842", "REACTOME:R-BTA-3371511", "REACTOME:R-BTA-6798695", "REACTOME:R-BTA-8876725", "REACTOME:R-CEL-3371511", "REACTOME:R-CEL-6798695", "REACTOME:R-CEL-8876725", "REACTOME:R-DDI-156842", "REACTOME:R-DDI-3371511", "REACTOME:R-DDI-6798695", "REACTOME:R-DDI-8876725", "REACTOME:...

41

[ "1f60", "1g7c", "1ije", "1ijf", "1jny", "1skq", "2b7b", "2b7c", "3vmf", "3wxm", "3wy9", "3wya", "4c0s", "4cxg", "4cxh", "5lzs", "5o8w", "6ji2", "6ra9", "6zmo", "7csl", "8b6z", "8g5z", "8g60", "8g6j", "8vvp", "8vvq", "8vvr", "8vvs", "8z70", "8z71", "9azc"...

34

[ "PUB00033951", "PUB00033952", "PUB00033953", "PUB00033960", "PUB00033961", "PUB00070083" ]

[ "12932732", "15922593", "12762045", "15680978", "12102560", "20974926" ]

[ "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "Structural studies of eukaryotic elongation factors.", "Recognition and selection of tRNA in translation.", "Mechanisms of EF-Tu, a pioneer GTPase.", "Omnipotent role of archaeal elongation factor 1 alpha (EF1α in trans...

[ 2003, 2005, 2001, 2005, 2002, 2010 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 1023, 9, 23602, 27 ]

4

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae (strai...

[ 6, 1, 20, 3, 39, 7, 1, 5, 8, 1, 3, 51 ]

12

true

Family

Translation elongation factor EF1A, eukaryotic/archaeal

Transl_elong_EF1A_euk/arc

6

IPR004540

4,540

Translation elongation factor EFG/EF2

Transl_elong_EFG/EF2

Family

35,609

false

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ , , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the pept...

[ "GO:0003746", "GO:0005525", "GO:0006414" ]

[ "translation elongation factor activity", "GTP binding", "translational elongation" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00054_B", "TIGR00484" ]

[ "EF_G_EF_2_B", "EF-G" ]

[ 33565, 35292 ]

2

[ "GP", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "GenProp0741", "R-CEL-5389840", "R-DME-5389840", "R-DRE-5389840", "R-HSA-5389840", "R-MMU-5389840", "R-RNO-5389840" ]

[ "GP:GenProp0741", "REACTOME:R-CEL-5389840", "REACTOME:R-DME-5389840", "REACTOME:R-DRE-5389840", "REACTOME:R-HSA-5389840", "REACTOME:R-MMU-5389840", "REACTOME:R-RNO-5389840" ]

7

[ "1dar", "1efg", "1elo", "1fnm", "1jqm", "1ktv", "1pn6", "1zn0", "2bm0", "2bm1", "2bv3", "2efg", "2j7k", "2om7", "2rdo", "2xex", "3izp", "3j0e", "3j9z", "3ja1", "3zz0", "3zzt", "3zzu", "4fn5", "4m1k", "4myt", "4myu", "4v5f", "4v5m", "4v5n", "4v6t", "4v7b"...

106

[ "PUB00014828", "PUB00033951", "PUB00033952", "PUB00033953" ]

[ "12471894", "12932732", "15922593", "12762045" ]

[ "Translational elongation factor G: a GTP-driven motor of the ribosome.", "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "Structural studies of eukaryotic elongation factors." ]

[ 2000, 2003, 2005, 2001 ]

4

[]

[ "IPR030848" ]

0

1

0

[ "Bacteria", "Eukaryota", "Methanobacteriota", "Viruses", "unclassified sequences" ]

[ 30020, 5224, 2, 2, 361 ]

5

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus",...

[ 10, 1, 1, 1, 1, 4, 1, 1, 4, 3, 1, 1, 14 ]

13

true

Family

Translation elongation factor EFG/EF2

Transl_elong_EFG/EF2

9

IPR004541

4,541

Translation elongation factor EFTu/EF1A, bacterial/organelle

Transl_elong_EFTu/EF1A_bac/org

Family

32,526

false

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [ , , ]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the pept...

[ "GO:0003746", "GO:0005525", "GO:0006414" ]

[ "translation elongation factor activity", "GTP binding", "translational elongation" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00118_B", "TIGR00485" ]

[ "EF_Tu_B", "EF-Tu" ]

[ 29076, 32475 ]

2

[ "EC", "GP", "REACTOME", "REACTOME" ]

[ "3.6.5.3", "GenProp0741", "R-HSA-5389840", "R-HSA-9754560" ]

[ "EC:3.6.5.3", "GP:GenProp0741", "REACTOME:R-HSA-5389840", "REACTOME:R-HSA-9754560" ]

4

[ "1aip", "1b23", "1d2e", "1d8t", "1dg1", "1efc", "1efm", "1eft", "1efu", "1etu", "1exm", "1ha3", "1ls2", "1mj1", "1ob2", "1ob5", "1qzd", "1ttt", "1tui", "1xb2", "1zc8", "2bvn", "2c77", "2c78", "2fx3", "2hcj", "2hdn", "3agp", "3agq", "3avt", "3avu", "3avv"...

134

[ "PUB00027704", "PUB00033951", "PUB00033952", "PUB00033953", "PUB00033960", "PUB00033961" ]

[ "16213500", "12932732", "15922593", "12762045", "15680978", "12102560" ]

[ "How can elongation factors EF-G and EF-Tu discriminate the functional state of the ribosome using the same binding site?", "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "Structural studies of eukaryotic elongation factors.", "Recognition and selection of tRNA in tran...

[ 2005, 2003, 2005, 2001, 2005, 2002 ]

6

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes code 15 clade", "Eukaryota", "unclassified sequences" ]

[ 4, 26446, 2, 5755, 319 ]

5

[ "Arabidopsis thaliana", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Saccharomyces cerevisiae...

[ 8, 1, 2, 2, 2, 1, 1, 4, 3, 1, 1, 13 ]

12

true

Family

Translation elongation factor EFTu/EF1A, bacterial/organelle

Transl_elong_EFTu/EF1A_bac/org

7

IPR004542

4,542

Translation elongation factor EF1B, beta chain, archaeal

Transl_elong_EF1B_B_arc

Family

890

false

This entry represents the beta (EF-1beta, also known as EF1B-alpha) chain of EF1B proteins from archaea (aEF-1beta). The beta chain has exchange activity, which mainly resides in its C-terminal region. In archaea, EF1B is a dimer [ ]. Translation elongation factors are responsible for two main processes during protein ...

[ "GO:0003746", "GO:0006414" ]

[ "translation elongation factor activity", "translational elongation" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "PIRSF", "PANTHER", "NCBIFAM" ]

[ "MF_00043", "PIRSF006521", "PTHR39647", "TIGR00489" ]

[ "EF1_beta", "Transl_elong_EF1B_B_arc", "", "aEF-1_beta" ]

[ 832, 744, 890, 803 ]

4

[]

0

[ "1gh8", "2yy3", "7csl" ]

3

[ "PUB00014829", "PUB00033951", "PUB00033952", "PUB00033953" ]

[ "8652615", "12932732", "15922593", "12762045" ]

[ "Archaeal elongation factor 1 beta is a dimer. Primary structure, molecular and biochemical properties.", "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "Structural studies of eukaryotic elongation factors." ]

[ 1996, 2003, 2005, 2001 ]

4

[]

0

null

[ "Archaea", "unclassified sequences" ]

[ 856, 34 ]

2

[]

0

true

Family

Translation elongation factor EF1B, beta chain, archaeal

Transl_elong_EF1B_B_arc

1

IPR004543

4,543

Translation elongation factor EFG/EF2, archaeal

Transl_elong_EFG/EF2_arc

Family

997

false

This entry represents archaeal EF2 proteins (also known as aEF2), which are more similar to eukaryotic EF2 than to bacterial EF2 (or EFG), both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylate...

[ "GO:0003746", "GO:0005525", "GO:0006414" ]

[ "translation elongation factor activity", "GTP binding", "translational elongation" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "HAMAP", "NCBIFAM" ]

[ "MF_00054_A", "TIGR00490" ]

[ "EF_G_EF_2_A", "aEF-2" ]

[ 837, 997 ]

2

[]

0

[ "5h7j", "5h7l", "6q2d", "6u43", "6u44", "6u45", "8hl1", "8hl2", "8hl3", "8hl4", "9ou7" ]

11

[ "PUB00033951", "PUB00033952", "PUB00033953", "PUB00033958", "PUB00033959" ]

[ "12932732", "15922593", "12762045", "12762009", "12762047" ]

[ "Elongation factors in protein biosynthesis.", "Elongation factors on the ribosome.", "Structural studies of eukaryotic elongation factors.", "Ratchet-like movements between the two ribosomal subunits: their implications in elongation factor recognition and tRNA translocation.", "Mechanism of elongation fac...

[ 2003, 2005, 2001, 2001, 2001 ]

5

[]

0

null

[ "Archaea", "unclassified sequences" ]

[ 984, 13 ]

2

[]

0

true

Family

Translation elongation factor EFG/EF2, archaeal

Transl_elong_EFG/EF2_arc

3

IPR004545

4,545

PA2G4 family

PA2G4

Family

2,948

false

Proteins of this family have been identified in a number of species as a nuclear protein with a cell cycle dependence. Various names have been given to members of this family which include cell cycle protein p38-2G4, also known as proliferation-associated protein PA2G4 [ , ], curved DNA-binding protein [ ], proliferati...

[]

0

[ "NCBIFAM" ]

[ "TIGR00495" ]

[ "crvDNA_42K" ]

[ 2948 ]

1

[ "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "R-DDI-6798695", "R-HSA-6798695", "R-MMU-6798695", "R-RNO-6798695", "R-SPO-6798695" ]

[ "REACTOME:R-DDI-6798695", "REACTOME:R-HSA-6798695", "REACTOME:R-MMU-6798695", "REACTOME:R-RNO-6798695", "REACTOME:R-SPO-6798695" ]

5

[ "2q8k", "2v6c", "3j2i", "6lsr", "6swa", "6sxo", "6wm8", "6z6l", "6z6m", "6z6n", "6zm7", "6zme", "6zmi", "6zmo", "7bhp", "7oya", "8k2c", "8uik", "8vvt", "8xsx", "8xsy", "8xsz", "9b0p" ]

23

[ "PUB00048899", "PUB00049595", "PUB00074549", "PUB00074550", "PUB00074552", "PUB00074555", "PUB00076723" ]

[ "17765895", "17690690", "7556453", "7985416", "24275324", "15073182", "9345902" ]

[ "The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions.", "Structural insights into the transcriptional and translational roles of Ebp1.", "Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4, which varies with the cell cycle.", "...

[ 2007, 2007, 1995, 1994, 2014, 2004, 1997 ]

7

[ "IPR047113" ]

[]

1

0

1

[ "Eukaryota" ]

[ 2948 ]

1

[ "Arabidopsis thaliana", "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Homo sapiens", "Mus musculus", "Oryza sativa subsp. japonica", "Rattus norvegicus", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "Zea mays" ]

[ 2, 1, 3, 2, 5, 4, 3, 2, 1, 6 ]

10

true

Family

PA2G4 family

PA2G4

4

IPR004546

4,546

Restriction endonuclease, type I, methylase subunit

Restrct_endonuc_T1M

Family

7,193

false

This entry represents the Type I restriction enzyme EcoR124II methylase subunit from Escherichia coli (T1M, also known as M subunit) and similar bacterial proteins. T1M functions in methylation of specific adenine residues, which is required for both restriction and modification activities [ , , , , ]. Methylation of s...

[ "GO:0003677", "GO:0009007", "GO:0009307" ]

[ "DNA binding", "site-specific DNA-methyltransferase (adenine-specific) activity", "DNA restriction-modification system" ]

[ "molecular_function", "molecular_function", "biological_process" ]

3

[ "NCBIFAM" ]

[ "TIGR00497" ]

[ "hsdM" ]

[ 7193 ]

1

[ "EC" ]

[ "2.1.1.72" ]

[ "EC:2.1.1.72" ]

1

[ "3lkd", "7bst", "7bto", "7btp", "7btq", "7btr" ]

6

[ "PUB00019721", "PUB00019722", "PUB00020851", "PUB00035705", "PUB00035706", "PUB00035707", "PUB00096663", "PUB00099965" ]

[ "11555298", "10449767", "8412658", "15121719", "12595133", "12665693", "32483229", "12654995" ]

[ "Analysis of type I restriction modification systems in the Neisseriaceae: genetic organization and properties of the gene products.", "Regulation of endonuclease activity by proteolysis prevents breakage of unmodified bacterial chromosomes by type I restriction enzymes.", "Conservation of motifs within the unu...

[ 2001, 1999, 1993, 2004, 2002, 2003, 2020, 2003 ]

8

[]

0

null

[ "Archaea", "Bacteria", "Caudoviricetes", "Eukaryota", "unclassified sequences" ]

[ 78, 7055, 3, 7, 50 ]

5

[]

0

true

Family

Restriction endonuclease, type I, methylase subunit

Restrct_endonuc_T1M

5

IPR004547

4,547

Glucosamine-6-phosphate isomerase

Glucosamine6P_isomerase

Family

22,472

false

Glucosamine-6-phosphate isomerase, aslo known as Glucosamine-6-phosphate deaminase ( ), catalyses the conversion of D-glucosamine 6-phosphate (GlcN6P) to D-fructose 6-phosphate and ammonium. This is the last step in the pathway for N-acetylglucosamine (GlcNAC) utilization in bacteria such as Escherichia coli (gene nagB...

[ "GO:0004342", "GO:0006044" ]

[ "glucosamine-6-phosphate deaminase activity", "N-acetylglucosamine metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "HAMAP", "PANTHER", "NCBIFAM", "CDD" ]

[ "MF_01241", "PTHR11280", "TIGR00502", "cd01399" ]

[ "GlcN6P_deamin", "", "nagB", "GlcN6P_deaminase" ]

[ 13794, 19484, 16078, 21218 ]

4

[ "EC", "GP", "METACYC", "METACYC", "METACYC", "PROSITEDOC", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME", "REACTOME" ]

[ "3.5.99.6", "GenProp1303", "PWY-5514", "PWY-6855", "PWY-6906", "PDOC00894", "R-BTA-70171", "R-CEL-70171", "R-DDI-70171", "R-DME-70171", "R-HSA-70171", "R-MMU-70171", "R-XTR-70171" ]

[ "EC:3.5.99.6", "GP:GenProp1303", "METACYC:PWY-5514", "METACYC:PWY-6855", "METACYC:PWY-6906", "PROSITEDOC:PDOC00894", "REACTOME:R-BTA-70171", "REACTOME:R-CEL-70171", "REACTOME:R-DDI-70171", "REACTOME:R-DME-70171", "REACTOME:R-HSA-70171", "REACTOME:R-MMU-70171", "REACTOME:R-XTR-70171" ]

13

[ "1cd5", "1dea", "1fqo", "1frz", "1fs5", "1fs6", "1fsf", "1hor", "1hot", "1jt9", "1ne7", "2bkv", "2bkx", "2ri0", "2ri1", "2wu1", "3hn6", "4r7t", "5hj5", "6nbg", "7lqm", "7lqn" ]

22

[ "PUB00005253", "PUB00044804" ]

[ "8747459", "18436239" ]

[ "Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.", "Ring-opening mechanism revealed by crystal structures of NagB and its ES intermediate complex." ]

[ 1995, 2008 ]

2

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "Marseillevirus LCMAC201", "unclassified sequences" ]

[ 6, 16819, 5421, 1, 225 ]

5

[ "Caenorhabditis elegans", "Danio rerio", "Drosophila melanogaster", "Escherichia coli (strain K12)", "Homo sapiens", "Mus musculus", "Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)", "Rattus norvegicus" ]

[ 1, 3, 3, 3, 11, 12, 1, 8 ]

8

true

Family

Glucosamine-6-phosphate isomerase

Glucosamine6P_isomerase

5

IPR004548

4,548

Peptide chain release factor 3

PrfC

Family

18,836

false

Peptide chain release factor 3 (RF-3, PrfC) is a GTPase found in a broad range of bacteria that accelerates dissociation of class I release factors (RF1 and RF2) from the ribosome following peptide release [ ]. In addition to its contribution to translation termination by recycling the class I release factors, RF3 has ...

[ "GO:0003924", "GO:0006415", "GO:0005737" ]

[ "GTPase activity", "translational termination", "cytoplasm" ]

[ "molecular_function", "biological_process", "cellular_component" ]

3

[ "HAMAP", "PANTHER", "NCBIFAM" ]

[ "MF_00072", "PTHR43556", "TIGR00503" ]

[ "Rel_fac_3", "", "prfC" ]

[ 17683, 18836, 17791 ]

3

[ "GP" ]

[ "GenProp0746" ]

[ "GP:GenProp0746" ]

1

[ "2h5e", "2o0f", "3tr5", "3vqt", "3vr1", "4v85", "4v89", "4v8o", "6gwt", "6gxm", "6gxn", "6gxo", "6gxp", "6lkq", "7m5d", "7siq", "8fzd", "8fzf", "8fzg", "8fzi", "8fzj" ]

21

[ "PUB00017445", "PUB00076473", "PUB00085744", "PUB00085745" ]

[ "9451005", "22000017", "27779391", "25636454" ]

[ "Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome.", "A primary role for release factor 3 in quality control during translation elongation in Escherichia coli.", "Mechanism of Translation Termination: RF1 Dissociation Follows Dissociation of ...

[ 1998, 2011, 2016, 2015 ]

4

[]

0

null

[ "Bacteria", "Eukaryota", "Myoviridae sp. cte0p10", "unclassified sequences" ]

[ 18353, 207, 1, 275 ]

4

[ "Escherichia coli (strain K12)" ]

[ 1 ]

1

true

Family

Peptide chain release factor 3

PrfC

5

IPR004549

4,549

Acetyl-CoA carboxylase, biotin carboxylase

Acetyl_CoA_COase_biotin_COase

Family

20,600

false

This family represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase ( ) is a heterohexamer of biotin carboxyl carrier protein, biotin carboxylase ( ), and two subunits of carboxyl transferase in a 2:2 complex. In the first step of long-chain fatty acid sy...

[ "GO:0016874" ]

[ "ligase activity" ]

[ "molecular_function" ]

1

[ "NCBIFAM" ]

[ "TIGR00514" ]

[ "accC" ]

[ 20600 ]

1

[ "EC", "GP", "GP", "METACYC", "METACYC", "METACYC" ]

[ "6.3.4.14", "GenProp0214", "GenProp1111", "PWY-5743", "PWY-5744", "PWY-5789" ]

[ "EC:6.3.4.14", "GP:GenProp0214", "GP:GenProp1111", "METACYC:PWY-5743", "METACYC:PWY-5744", "METACYC:PWY-5789" ]

6

[ "1bnc", "1dv1", "1dv2", "1ulz", "2c00", "2gps", "2gpw", "2j9g", "2v58", "2v59", "2v5a", "2vpq", "2vqd", "2vr1", "2w6m", "2w6n", "2w6o", "2w6p", "2w6q", "2w6z", "2w70", "2w71", "3g8c", "3g8d", "3jzf", "3jzi", "3ouu", "3ouz", "3rup", "3rv3", "3rv4", "4hr7"...

52

[]

0

[]

0

null

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 237, 19514, 665, 184 ]

4

[ "Arabidopsis thaliana", "Escherichia coli (strain K12)" ]

[ 7, 1 ]

2

true

Family

Acetyl-CoA carboxylase, biotin carboxylase

Acetyl_CoA_COase_biotin_COase

7

IPR004550

4,550

L-asparaginase, type II

AsnASE_II

Family

13,514

false

L-asparaginase catalyses the conversion of L-asparagine to L-aspartate. Two related families of asparaginase (L-asparagine amidohydrolase, ) are designated type I and type II according to the terminology in Escherichia coli, which has both: L-asparaginase I is a low-affinity enzyme found in the cytoplasm, while L-aspar...

[ "GO:0004067", "GO:0006528" ]

[ "asparaginase activity", "asparagine metabolic process" ]

[ "molecular_function", "biological_process" ]

2

[ "NCBIFAM", "CDD" ]

[ "TIGR00520", "cd08964" ]

[ "asnASE_II", "L-asparaginase_II" ]

[ 5828, 11905 ]

2

[ "EC", "GP", "METACYC" ]

[ "3.5.1.1", "GenProp1404", "PWY-8402" ]

[ "EC:3.5.1.1", "GP:GenProp1404", "METACYC:PWY-8402" ]

3

[ "1agx", "1djo", "1djp", "1hfj", "1hfk", "1hfw", "1hg0", "1hg1", "1ho3", "1ihd", "1jaz", "1jja", "1jsl", "1jsr", "1nns", "1o7j", "1wsa", "1zcf", "2gvn", "2hln", "2jk0", "2wlt", "2wt4", "3eca", "3nxk", "3pga", "4eca", "4pga", "5f52", "5hw0", "5i3z", "5i48"...

115

[ "PUB00033038", "PUB00085037", "PUB00091779", "PUB00091780" ]

[ "8706862", "11996000", "21769889", "6992886" ]

[ "A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant.", "Sequence analysis of enzymes with asparaginase activity.", "Proteins from Erwinia asparaginase Erwinase ® and E. coli asparaginase 2 MEDAC ® for treatment of human leukemia, show a multitude...

[ 1996, 2001, 2011, 1980 ]

4

[ "IPR006034" ]

[]

1

0

1

[ "Archaea", "Bacteria", "Eukaryota", "unclassified sequences" ]

[ 203, 12065, 1181, 65 ]

4

[ "Escherichia coli (strain K12)", "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "Schizosaccharomyces pombe (strain 972 / ATCC 24843)" ]

[ 1, 5, 4 ]

3

true

Family

L-asparaginase, type II

AsnASE_II

2